|
Name |
Accession |
Description |
Interval |
E-value |
| PRK09124 |
PRK09124 |
ubiquinone-dependent pyruvate dehydrogenase; |
1-572 |
0e+00 |
|
ubiquinone-dependent pyruvate dehydrogenase;
Pssm-ID: 181661 [Multi-domain] Cd Length: 574 Bit Score: 1184.01 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 1 MKQTVAAYIAKTLEQAGVKRIWGVTGDSLNGLSDSLNRMGTIDWMPTRHEEVAAFAAGAEAQLTGELAVCAGSCGPGNLH 80
Cdd:PRK09124 1 MKQTVADYIAKTLEQAGVKRIWGVTGDSLNGLSDSLRRMGTIEWMHTRHEEVAAFAAGAEAQLTGELAVCAGSCGPGNLH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 81 LINGLFDCHRNHVPVLAIAAHIPSSEIGSGYFQETHPQELFRECSHYCELVSTPEQIPQVLAIAMRKAVINRGVSVVVLP 160
Cdd:PRK09124 81 LINGLFDCHRNHVPVLAIAAHIPSSEIGSGYFQETHPQELFRECSHYCELVSNPEQLPRVLAIAMRKAILNRGVAVVVLP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 161 GDVALKAAPESASSHWYHAPLPQVTPAEEELKKLAQLLRYSSNIALMCGSGCAGAHKELVDFAAKLKAPIVHALRGKEHV 240
Cdd:PRK09124 161 GDVALKPAPERATPHWYHAPQPVVTPAEEELRKLAALLNGSSNITLLCGSGCAGAHDELVALAETLKAPIVHALRGKEHV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 241 EYDNPYDVGMTGLIGFSSGFHTMMNADTLVLLGTQFPYRAFYPTDAKIIQIDINPGSIGAHSKVDMALVGDIKSTLSALM 320
Cdd:PRK09124 241 EYDNPYDVGMTGLIGFSSGYHAMMNCDTLLMLGTDFPYRQFYPTDAKIIQIDINPGSLGRRSPVDLGLVGDVKATLAALL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 321 PHLEEKTDRKFLDKALEHYRDARKGLDDLAKPSD--KTIHPQYLAQRISHYADDDAIFTCDVGTPTVWAARYLQMNGKRR 398
Cdd:PRK09124 321 PLLEEKTDRKFLDKALEHYRKARKGLDDLAVPSDggKPIHPQYLARQISEFAADDAIFTCDVGTPTVWAARYLKMNGKRR 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 399 LLGSFNHGSMANAMPQAIGAKATAPDRQVVAMCGDGGFSMLMGDFLSLAQMKLPVKIVIFNNSVLGFVAMEMKAGGYLTD 478
Cdd:PRK09124 401 LLGSFNHGSMANAMPQALGAQAAHPGRQVVALSGDGGFSMLMGDFLSLVQLKLPVKIVVFNNSVLGFVAMEMKAGGYLTD 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 479 GTELHATNFARIAEACGIKGIRVESASEVDEALQTAFATDGPVLVDVVVASEELAMPPQIKLEQAKGFSLYMLRAIISGR 558
Cdd:PRK09124 481 GTDLHNPDFAAIAEACGITGIRVEKASELDGALQRAFAHDGPALVDVVTAKQELAMPPQIKLEQAKGFSLYMLRAIISGR 560
|
570
....*....|....
gi 640683833 559 GDEVIELAKTNWLR 572
Cdd:PRK09124 561 GDEVIELAKTNWLR 574
|
|
| PRK06546 |
PRK06546 |
pyruvate dehydrogenase; Provisional |
1-572 |
0e+00 |
|
pyruvate dehydrogenase; Provisional
Pssm-ID: 180614 [Multi-domain] Cd Length: 578 Bit Score: 751.05 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 1 MKQTVAAYIAKTLEQAGVKRIWGVTGDSLNGLSDSLNRMGTIDWMPTRHEEVAAFAAGAEAQLTGELAVCAGSCGPGNLH 80
Cdd:PRK06546 1 MAKTVAEQLVEQLVAAGVKRIYGIVGDSLNPIVDAVRRTGGIEWVHVRHEEAAAFAAAAEAQLTGKLAVCAGSCGPGNLH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 81 LINGLFDCHRNHVPVLAIAAHIPSSEIGSGYFQETHPQELFRECSHYCELVSTPEQIPQVLAIAMRKAVINRGVSVVVLP 160
Cdd:PRK06546 81 LINGLYDAHRSGAPVLAIASHIPSAQIGSGFFQETHPDRLFVECSGYCEMVSSAEQAPRVLHSAIQHAVAGGGVSVVTLP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 161 GDVALKAAPESASSHWYHAPLPQVTPAEEELKKLAQLLRYSSNIALMCGSGCAGAHKELVDFAAKLKAPIVHALRGKEHV 240
Cdd:PRK06546 161 GDIADEPAPEGFAPSVISPRRPTVVPDPAEVRALADAINEAKKVTLFAGAGVRGAHAEVLALAEKIKAPVGHSLRGKEWI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 241 EYDNPYDVGMTGLIGFSSGFHTMMNADTLVLLGTQFPYRAFYPtDAKIIQIDINPGSIGAHSKVDMALVGDIKSTLSALM 320
Cdd:PRK06546 241 QYDNPFDVGMSGLLGYGAAHEAMHEADLLILLGTDFPYDQFLP-DVRTAQVDIDPEHLGRRTRVDLAVHGDVAETIRALL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 321 PHLEEKTDRKFLDKAL-EHYRDARKGLDDLAKPSDKT--IHPQYLAQRISHYADDDAIFTCDVGTPTVWAARYLQMNGKR 397
Cdd:PRK06546 320 PLVKEKTDRRFLDRMLkKHARKLEKVVGAYTRKVEKHtpIHPEYVASILDELAADDAVFTVDTGMCNVWAARYITPNGRR 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 398 RLLGSFNHGSMANAMPQAIGAKATAPDRQVVAMCGDGGFSMLMGDFLSLAQMKLPVKIVIFNNSVLGFVAMEMKAGGYLT 477
Cdd:PRK06546 400 RVIGSFRHGSMANALPHAIGAQLADPGRQVISMSGDGGLSMLLGELLTVKLYDLPVKVVVFNNSTLGMVKLEMLVDGLPD 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 478 DGTELHATNFARIAEACGIKGIRVESASEVDEALQTAFATDGPVLVDVVVASEELAMPPQIKLEQAKGFSLYMLRAIISG 557
Cdd:PRK06546 480 FGTDHPPVDYAAIAAALGIHAVRVEDPKDVRGALREAFAHPGPALVDVVTDPNALSIPPTITGEQVKGFALAASKTVLNG 559
|
570
....*....|....*
gi 640683833 558 RGDEVIELAKTNwLR 572
Cdd:PRK06546 560 GVGEMVDMARSN-LR 573
|
|
| IlvB |
COG0028 |
Acetolactate synthase large subunit or other thiamine pyrophosphate-requiring enzyme [Amino ... |
1-539 |
0e+00 |
|
Acetolactate synthase large subunit or other thiamine pyrophosphate-requiring enzyme [Amino acid transport and metabolism, Coenzyme transport and metabolism]; Acetolactate synthase large subunit or other thiamine pyrophosphate-requiring enzyme is part of the Pathway/BioSystem: Isoleucine, leucine, valine biosynthesis
Pssm-ID: 439799 [Multi-domain] Cd Length: 548 Bit Score: 552.46 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 1 MKQTVAAYIAKTLEQAGVKRIWGVTGDSLNGLSDSLNRMGTIDWMPTRHEEVAAFAAGAEAQLTGELAVCAGSCGPGNLH 80
Cdd:COG0028 1 MKMTGADALVEALEAEGVETVFGVPGGAILPLYDALRRQSGIRHILVRHEQGAAFMADGYARATGKPGVCLVTSGPGATN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 81 LINGLFDCHRNHVPVLAIAAHIPSSEIGSGYFQETHPQELFRECSHYCELVSTPEQIPQVLAIAMRKAVINR-GVSVVVL 159
Cdd:COG0028 81 LVTGLADAYMDSVPVLAITGQVPTSLIGRGAFQEVDQVGLFRPITKWSYLVTDPEDLPEVLRRAFRIATSGRpGPVVLDI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 160 PGDVALKAAPESASSHWYHAPLPQVTPAEEELKKLAQLLRYSSNIALMCGSGC--AGAHKELVDFAAKLKAPIVHALRGK 237
Cdd:COG0028 161 PKDVQAAEAEEEPAPPELRGYRPRPAPDPEAIEEAAELLAAAKRPVILAGGGArrAGAAEELRALAERLGAPVVTTLMGK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 238 EHVEYDNPYDVGMTGLIGFSSGFHTMMNADTLVLLGTQFPYR------AFYPtDAKIIQIDINPGSIGAHSKVDMALVGD 311
Cdd:COG0028 241 GAFPEDHPLYLGMLGMHGTPAANEALAEADLVLAVGARFDDRvtgnwdEFAP-DAKIIHIDIDPAEIGKNYPVDLPIVGD 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 312 IKSTLSALMPHLEEKTDRKflDKALEHYRDARKGLDDLAKPSDKTIHPQYLAQRISHYADDDAIFTCDVGTPTVWAARYL 391
Cdd:COG0028 320 AKAVLAALLEALEPRADDR--AAWLARIAAWRAEYLAAYAADDGPIKPQRVIAALREALPDDAIVVTDVGQHQMWAARYL 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 392 QMNGKRRLLGSFNHGSMANAMPQAIGAKATAPDRQVVAMCGDGGFSMLMGDFLSLAQMKLPVKIVIFNNSVLGFVAMEMK 471
Cdd:COG0028 398 RFRRPRRFLTSGGLGTMGYGLPAAIGAKLARPDRPVVAITGDGGFQMNLQELATAVRYGLPVKVVVLNNGGLGMVRQWQE 477
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 640683833 472 A-GGYLTDGTELHATNFARIAEACGIKGIRVESASEVDEALQTAFATDGPVLVDVVVASEELAMPPQIK 539
Cdd:COG0028 478 LfYGGRYSGTDLPNPDFAKLAEAFGAKGERVETPEELEAALEEALASDGPALIDVRVDPEENPPGATLD 546
|
|
| PRK08611 |
PRK08611 |
pyruvate oxidase; Provisional |
1-555 |
8.95e-164 |
|
pyruvate oxidase; Provisional
Pssm-ID: 181502 [Multi-domain] Cd Length: 576 Bit Score: 478.73 E-value: 8.95e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 1 MKQTVAAYIAKTLEQAGVKRIWGVTGDSLNGLSDSLNRM-GTIDWMPTRHEEVAAFAAGAEAQLTGELAVCAGSCGPGNL 79
Cdd:PRK08611 2 AKIKAGEALVKLLQDWGIDHVYGIPGDSIDAVVDALRKEqDKIKFIQVRHEEVAALAAAAYAKLTGKIGVCLSIGGPGAI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 80 HLINGLFDCHRNHVPVLAIAAHIPSSEIGSGYFQETHPQELFRECSHYCELVSTPEQIPQVLAIAMRKAVINRGVSVVVL 159
Cdd:PRK08611 82 HLLNGLYDAKMDHVPVLALAGQVTSDLLGTDFFQEVNLEKMFEDVAVYNHQIMSAENLPEIVNQAIRTAYEKKGVAVLTI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 160 PGDV---ALKAAPESASSHWyhaPLPQVTPAEEELKKLAQLLRYSSNIALMCGSGCAGAHKELVDFAAKLKAPIVHALRG 236
Cdd:PRK08611 162 PDDLpaqKIKDTTNKTVDTF---RPTVPSPKPKDIKKAAKLINKAKKPVILAGLGAKHAKEELLAFAEKAKIPIIHTLPA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 237 KEHVEYDNPYDVGMTGLIGFSSGFHTMMNADTLVLLGTQFPYRAFYPTDAKIIQIDINPGSIGAHSKVDMALVGDIKSTL 316
Cdd:PRK08611 239 KGIIPDDHPYSLGNLGKIGTKPAYEAMQEADLLIMVGTNYPYVDYLPKKAKAIQIDTDPANIGKRYPVNVGLVGDAKKAL 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 317 SALMPHLEEKTDRKFLDKALEHYRDARKGLD-DLAKPSDKtIHPQYLAQRISHYADDDAIFTCDVGTPTVWAARYLQMNG 395
Cdd:PRK08611 319 HQLTENIKHVEDRRFLEACQENMAKWWKWMEeDENNASTP-IKPERVMAAIQKIADDDAVLSVDVGTVTVWSARYLNLGT 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 396 KRRLLGSFNHGSMANAMPQAIGAKATAPDRQVVAMCGDGGFSMLMGDFLSLAQMKLPVKIVIFNNSVLGFVAMEMKAGGY 475
Cdd:PRK08611 398 NQKFIISSWLGTMGCGLPGAIAAKIAFPDRQAIAICGDGGFSMVMQDFVTAVKYKLPIVVVVLNNQQLAFIKYEQQAAGE 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 476 LTDGTELHATNFARIAEACGIKGIRVESASEVDEALQTAFATDGPVLVDVVVASEELAMPPQIKLEQAKGFSLYMLRAII 555
Cdd:PRK08611 478 LEYAIDLSDMDYAKFAEACGGKGYRVEKAEELDPAFEEALAQDKPVIIDVYVDPNAAPLPGKIVNDEALGYSKWAIKSLF 557
|
|
| PRK06457 |
PRK06457 |
pyruvate dehydrogenase; Provisional |
4-558 |
2.28e-137 |
|
pyruvate dehydrogenase; Provisional
Pssm-ID: 180570 [Multi-domain] Cd Length: 549 Bit Score: 409.99 E-value: 2.28e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 4 TVAAYIAKTLEQAGVKRIWGVTGDSLNGLSDSLnRMGTIDWMPTRHEEVAAFAAGAEAQLTGELAVCAGSCGPGNLHLIN 83
Cdd:PRK06457 3 SVAEVIIRVLEDNGIQRIYGIPGDSIDPLVDAI-RKSKVKYVQVRHEEGAALAASVEAKITGKPSACMGTSGPGSIHLLN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 84 GLFDCHRNHVPVLAIAAHIPSSEIGSGYFQETHPQELFRECSHYCELVSTPEQIPQVLAIAMRKAVINRGVSVVVLPGDV 163
Cdd:PRK06457 82 GLYDAKMDHAPVIALTGQVESDMIGHDYFQEVNLTKLFDDVAVFNQILINPENAEYIIRRAIREAISKRGVAHINLPVDI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 164 aLKAAPESASSHWYHAPLPQVTPaeeELKKLAQLLRYSSNIALMCGSGCAGAHKELVDFAAKLKAPIVHALRGKEHVEYD 243
Cdd:PRK06457 162 -LRKSSEYKGSKNTEVGKVKYSI---DFSRAKELIKESEKPVLLIGGGTRGLGKEINRFAEKIGAPIIYTLNGKGILPDL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 244 NPYDVGMTGLIGFSSGFHTMMNADTLVLLGTQFPYRAFYPTDAKIIQIDINPGSIGAHSKVDMALVGDIKSTLSalmPHL 323
Cdd:PRK06457 238 DPKVMGGIGLLGTKPSIEAMDKADLLIMLGTSFPYVNFLNKSAKVIQVDIDNSNIGKRLDVDLSYPIPVAEFLN---IDI 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 324 EEKTDrKFLDKALEHYRDARKGLDDLAKPSDKTIHPQYLAQRISHYADDDAIFTCDVGTPTVWAARYLQMNGKRRLLGSF 403
Cdd:PRK06457 315 EEKSD-KFYEELKGKKEDWLDSISKQENSLDKPMKPQRVAYIVSQKCKKDAVIVTDTGNVTMWTARHFRASGEQTFIFSA 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 404 NHGSMANAMPQAIGAK-ATAPDRQVVAMCGDGGFSMLMGDFLSLAQMKLPVKIVIFNNSVLGFVAMEMKAGGYLTDGTEL 482
Cdd:PRK06457 394 WLGSMGIGVPGSVGASfAVENKRQVISFVGDGGFTMTMMELITAKKYDLPVKIIIYNNSKLGMIKFEQEVMGYPEWGVDL 473
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 640683833 483 HATNFARIAEACGIKGIRVESASEVDEALQTAFATDGPVLVDVVVASEELAMPPQIKLEQAKGFSLYMLRAIISGR 558
Cdd:PRK06457 474 YNPDFTKIAESIGFKGFRLEEPKEAEEIIEEFLNTKGPAVLDAIVDPNERPMPPKLTFKQAGEYVLSIFREKLEGI 549
|
|
| PRK08273 |
PRK08273 |
thiamine pyrophosphate protein; Provisional |
1-570 |
8.58e-121 |
|
thiamine pyrophosphate protein; Provisional
Pssm-ID: 181344 [Multi-domain] Cd Length: 597 Bit Score: 368.85 E-value: 8.58e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 1 MKQTVAAYIAKTLEQAGVKRIWGVTGDSLNGLSDSLNRM-GTIDWMPTRHEEVAAFAAGAEAQLTGELAVCAGSCGPGNL 79
Cdd:PRK08273 1 MSQTVADFILERLREWGVRRVFGYPGDGINGLLGALGRAdDKPEFVQARHEEMAAFMAVAHAKFTGEVGVCLATSGPGAI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 80 HLINGLFDCHRNHVPVLAIAAHIPSSEIGSGYFQETHPQELFRECSH-YCELVSTPEQIPQVLAIAMRKAVINRGVSVVV 158
Cdd:PRK08273 81 HLLNGLYDAKLDHVPVVAIVGQQARAALGGHYQQEVDLQSLFKDVAGaFVQMVTVPEQLRHLVDRAVRTALAERTVTAVI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 159 LPGDVALKAAPESASSHWY-----HAPLPQVTPAEEELKKLAQLLRYSSNIALMCGSGCAGAHKELVDFAAKLKAPIVHA 233
Cdd:PRK08273 161 LPNDVQELEYEPPPHAHGTvhsgvGYTRPRVVPYDEDLRRAAEVLNAGRKVAILVGAGALGATDEVIAVAERLGAGVAKA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 234 LRGKEHVEYDNPYDVGMTGLIGFSSGFHTMMNADTLVLLGTQFPYRAFYPT--DAKIIQIDINPGSIGAHSKVDMALVGD 311
Cdd:PRK08273 241 LLGKAALPDDLPWVTGSIGLLGTKPSYELMRECDTLLMVGSSFPYSEFLPKegQARGVQIDIDGRMLGLRYPMEVNLVGD 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 312 IKSTLSALMPHLEEKTDRKFLDKALEHYRDARKGLDDLAKPSDKTIHPQYLAQRISHYADDDAIFTCDVGTPTVWAARYL 391
Cdd:PRK08273 321 AAETLRALLPLLERKKDRSWRERIEKWVARWWETLEARAMVPADPVNPQRVFWELSPRLPDNAILTADSGSCANWYARDL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 392 QMngKRRLLGSFNHG--SMANAMPQAIGAKATAPDRQVVAMCGDGGFSML-MGDFLSLA----QMKLPVKIV-IFNNSVL 463
Cdd:PRK08273 401 RM--RRGMMASLSGTlaTMGPAVPYAIAAKFAHPDRPVIALVGDGAMQMNgMAELITVAkywrQWSDPRLIVlVLNNRDL 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 464 GFVAMEMKA-GG--YLTDGTELHATNFARIAEACGIKGIRVESASEVDEALQTAFATDGPVLVDVVVASEELAMPPQIKL 540
Cdd:PRK08273 479 NQVTWEQRVmEGdpKFEASQDLPDVPYARFAELLGLKGIRVDDPEQLGAAWDEALAADRPVVLEVKTDPNVPPLPPHITL 558
|
570 580 590
....*....|....*....|....*....|...
gi 640683833 541 EQAKGFslymLRAIISGRGDE---VIELAKTNW 570
Cdd:PRK08273 559 EQAKAF----ASALLKGDPDAggvIVQTAKQVL 587
|
|
| pyruv_oxi_spxB |
TIGR02720 |
pyruvate oxidase; Members of this family are examples of pyruvate oxidase (EC 1.2.3.3), an ... |
6-527 |
5.20e-105 |
|
pyruvate oxidase; Members of this family are examples of pyruvate oxidase (EC 1.2.3.3), an enzyme with FAD and TPP as cofactors that catalyzes the reaction pyruvate + phosphate + O2 + H2O = acetyl phosphate + CO2 + H2O2. It should not be confused with pyruvate dehydrogenase [cytochrome] (EC 1.2.2.2) as in E. coli PoxB, although the E. coli enzyme is closely homologous and has pyruvate oxidase as an alternate name. [Energy metabolism, Aerobic]
Pssm-ID: 213733 [Multi-domain] Cd Length: 575 Bit Score: 327.56 E-value: 5.20e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 6 AAYIAKTLEQAGVKRIWGVTGDSLNGLSDSL-NRMGTIDWMPTRHEEVAAFAAGAEAQLTGELAVCAGSCGPGNLHLING 84
Cdd:TIGR02720 2 SAAVLKVLEAWGVDHIYGIPGGSFNSTMDALsAERDRIHYIQVRHEEVGALAAAADAKLTGKIGVCFGSAGPGATHLLNG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 85 LFDCHRNHVPVLAIAAHIPSSEIGSGYFQETHPQELFRECSHYCELVSTPEQIPQVLAIAMRKAVINRGVSVVVLPGDVA 164
Cdd:TIGR02720 82 LYDAKEDHVPVLALVGQVPTTGMNMDTFQEMNENPIYADVAVYNRTAMTAESLPHVIDEAIRRAYAHNGVAVVTIPVDFG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 165 LKAAPE----SASSHWYHAPLPqvTPAEEELKKLAQLLRYSSNIALMCGSGCAGAHKELVDFAAKLKAPIVHALRGKEHV 240
Cdd:TIGR02720 162 WQEIPDndyyASSVSYQTPLLP--APDVEAVTRAVQTLKAAERPVIYYGIGARKAGEELEALSEKLKIPLISTGLAKGII 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 241 EYDNPYDVGMTGLIGFSSGFHTMMNADTLVLLGTQFPYRAFYPT--DAK-IIQIDINPGSIGAHSKVDMALVGDIKSTLS 317
Cdd:TIGR02720 240 EDRYPAYLGSAYRVAQKPANEALFQADLVLFVGNNYPFAEVSKAfkNTKyFIQIDIDPAKLGKRHHTDIAVLADAKKALA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 318 ALMPHLEEKTDRKFLDKALEHYRDARKGLDDLAKPSDKTIHPQYLAQRISHYADDDAIFTCDVGTPTVWAARYLQMNGKR 397
Cdd:TIGR02720 320 AILAQVEPRESTPWWQANVANVKNWRAYLASLEDKTEGPLQAYQVYRAINKIAEDDAIYSIDVGDININSNRHLKMTPKN 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 398 RLLGSFNHGSMANAMPQAIGAKATAPDRQVVAMCGDGGFSMLMGDFLSLAQMKLPVKIVIFNNSVLGFVAMEMKAGGYLT 477
Cdd:TIGR02720 400 KWITSNLFATMGVGVPGAIAAKLNYPDRQVFNLAGDGAFSMTMQDLLTQVQYHLPVINIVFSNCTYGFIKDEQEDTNQPL 479
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 640683833 478 DGTELHATNFARIAEACGIKGIRVESASEVDEALQTA--FATDGPVLVDVVV 527
Cdd:TIGR02720 480 IGVDFNDADFAKIAEGVGAVGFRVNKIEQLPAVFEQAkaIKQGKPVLIDAKI 531
|
|
| acolac_lg |
TIGR00118 |
acetolactate synthase, large subunit, biosynthetic type; Two groups of proteins form ... |
3-538 |
2.68e-98 |
|
acetolactate synthase, large subunit, biosynthetic type; Two groups of proteins form acetolactate from two molecules of pyruvate. The type of acetolactate synthase described in this model also catalyzes the formation of acetohydroxybutyrate from pyruvate and 2-oxobutyrate, an early step in the branched chain amino acid biosynthesis; it is therefore also termed acetohydroxyacid synthase. In bacteria, this catalytic chain is associated with a smaller regulatory chain in an alpha2/beta2 heterotetramer. Acetolactate synthase is a thiamine pyrophosphate enzyme. In this type, FAD and Mg++ are also found. Several isozymes of this enzyme are found in E. coli K12, one of which contains a frameshift in the large subunit gene and is not expressed. [Amino acid biosynthesis, Pyruvate family]
Pssm-ID: 272915 [Multi-domain] Cd Length: 558 Bit Score: 309.73 E-value: 2.68e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 3 QTVAAYIAKTLEQAGVKRIWGVTGDSLNGLSDSLNRMGTIDWMPTRHEEVAAFAAGAEAQLTGELAVCAGSCGPGNLHLI 82
Cdd:TIGR00118 1 MSGAEAIIESLKDEGVKTVFGYPGGAILPIYDALYNDSGIEHILVRHEQGAAHAADGYARASGKVGVVLVTSGPGATNLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 83 NGLFDCHRNHVPVLAIAAHIPSSEIGSGYFQETHPQELFRECSHYCELVSTPEQIPQVLAIAMRKAVINRGVSVVV-LPG 161
Cdd:TIGR00118 81 TGIATAYMDSIPMVVFTGQVPTSLIGSDAFQEADILGITMPITKHSFQVKSAEDIPRIIKEAFHIATTGRPGPVLVdLPK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 162 DVALKAA----PESASSHWYHaplPQVTPAEEELKKLAQLLRYSSNIALMCGSGC--AGAHKELVDFAAKLKAPIVHALR 235
Cdd:TIGR00118 161 DVTTAEIeypyPEKVNLPGYR---PTVKGHPLQIKKAAELINLAKKPVILVGGGViiAGASEELKELAERIQIPVTTTLM 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 236 GKEHVEYDNPYDVGMTGLIGFSSGFHTMMNADTLVLLGTQFPYR-----AFYPTDAKIIQIDINPGSIGAHSKVDMALVG 310
Cdd:TIGR00118 238 GLGSFPEDHPLSLGMLGMHGTKTANLAVHECDLIIAVGARFDDRvtgnlAKFAPNAKIIHIDIDPAEIGKNVRVDIPIVG 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 311 DIKSTLSALMPHLEEKTDRKFLD--KALEHYRdARKGLDdlAKPSDKTIHPQYLAQRISHYADDDAIFTCDVGTPTVWAA 388
Cdd:TIGR00118 318 DARNVLEELLKKLFELKERKESAwlEQINKWK-KEYPLK--MDYTEEGIKPQQVIEELSRVTKDEAIVTTDVGQHQMWAA 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 389 RYLQMNGKRRLLGSFNHGSMANAMPQAIGAKATAPDRQVVAMCGDGGFSMLMGDFLSLAQMKLPVKIVIFNNSVLGFVA- 467
Cdd:TIGR00118 395 QFYPFRKPRRFITSGGLGTMGFGLPAAIGAKVAKPESTVICITGDGSFQMNLQELSTAVQYDIPVKILILNNRYLGMVRq 474
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 640683833 468 -MEMKAGGYLTDGTELHATNFARIAEACGIKGIRVESASEVDEALQTAFATDGPVLVDVVVASEELAMPPQI 538
Cdd:TIGR00118 475 wQELFYEERYSHTHMGSLPDFVKLAEAYGIKGIRIEKPEELDEKLKEALSSNEPVLLDVVVDKPENVLPMVA 546
|
|
| TPP_POX |
cd02014 |
Thiamine pyrophosphate (TPP) family, Pyruvate oxidase (POX) subfamily, TPP-binding module; ... |
357-533 |
1.82e-96 |
|
Thiamine pyrophosphate (TPP) family, Pyruvate oxidase (POX) subfamily, TPP-binding module; composed of proteins similar to Lactobacillus plantarum POX, which plays a key role in controlling acetate production under aerobic conditions. POX decarboxylates pyruvate, producing hydrogen peroxide and the energy-storage metabolite acetylphosphate. It requires FAD in addition to TPP and a divalent cation as cofactors.
Pssm-ID: 238972 [Multi-domain] Cd Length: 178 Bit Score: 291.36 E-value: 1.82e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 357 IHPQYLAQRISHYADDDAIFTCDVGTPTVWAARYLQMNGKRRLLGSFNHGSMANAMPQAIGAKATAPDRQVVAMCGDGGF 436
Cdd:cd02014 2 IHPERVAAELNKRAPDDAIFTIDVGNVTVWAARHLRMNGKQRFILSGLLATMGNGLPGAIAAKLAYPDRQVIALSGDGGF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 437 SMLMGDFLSLAQMKLPVKIVIFNNSVLGFVAMEMKAGGYLTDGTELHATNFARIAEACGIKGIRVESASEVDEALQTAFA 516
Cdd:cd02014 82 AMLMGDLITAVKYNLPVIVVVFNNSDLGFIKWEQEVMGQPEFGVDLPNPDFAKIAEAMGIKGIRVEDPDELEAALDEALA 161
|
170
....*....|....*..
gi 640683833 517 TDGPVLVDVVVASEELA 533
Cdd:cd02014 162 ADGPVVIDVVTDPNEPP 178
|
|
| PRK06276 |
PRK06276 |
acetolactate synthase large subunit; |
9-540 |
2.01e-81 |
|
acetolactate synthase large subunit;
Pssm-ID: 235766 [Multi-domain] Cd Length: 586 Bit Score: 266.23 E-value: 2.01e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 9 IAKTLEQAGVKRIWGVTGDSLNGLSDSLNRmGTIDWMPTRHEEVAAFAAGAEAQLTGELAVCAGSCGPGNLHLINGLFDC 88
Cdd:PRK06276 7 IIKALEAEGVKIIFGYPGGALLPFYDALYD-SDLIHILTRHEQAAAHAADGYARASGKVGVCVATSGPGATNLVTGIATA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 89 HRNHVPVLAIAAHIPSSEIGSGYFQETHPQELFRECSHYCELVSTPEQIPQVLAIAMRKAVINRGVSVVV-LPGDVALKA 167
Cdd:PRK06276 86 YADSSPVIALTGQVPTKLIGNDAFQEIDALGIFMPITKHNFQIKKPEEIPEIFRAAFEIAKTGRPGPVHIdLPKDVQEGE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 168 APESASSHWYHAPLPQVTPAEE----ELKKLAQLLRYSSNIALMCGSGC--AGAHKELVDFAAKLKAPIVHALRGKEHVE 241
Cdd:PRK06276 166 LDLEKYPIPAKIDLPGYKPTTFghplQIKKAAELIAEAERPVILAGGGViiSGASEELIELSELVKIPVCTTLMGKGAFP 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 242 YDNPYDVGMTGLIGFSSGFHTMMNADTLVLLGTQFPYRA------FYPtDAKIIQIDINPGSIGAHSKVDMALVGDIKST 315
Cdd:PRK06276 246 EDHPLALGMVGMHGTKAANYSVTESDVLIAIGCRFSDRTtgdissFAP-NAKIIHIDIDPAEIGKNVRVDVPIVGDAKNV 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 316 LSALMPHLEEKtDRKFLDKALEHYRDARKGLDDLAKPSDKTIHPQYLAQRISHYADD-----DAIFTCDVGTPTVWAARY 390
Cdd:PRK06276 325 LRDLLAELMKK-EIKNKSEWLERVKKLKKESIPRMDFDDKPIKPQRVIKELMEVLREidpskNTIITTDVGQNQMWMAHF 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 391 LQMNGKRRLLGSFNHGSMANAMPQAIGAKATAPDRQVVAMCGDGGFSMLMGDFLSLAQMKLPVKIVIFNNSVLGFVAmEM 470
Cdd:PRK06276 404 FKTSAPRSFISSGGLGTMGFGFPAAIGAKVAKPDANVIAITGDGGFLMNSQELATIAEYDIPVVICIFDNRTLGMVY-QW 482
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 640683833 471 KAGGYLTDGTELH---ATNFARIAEACGIKGIRVESASEVDEALQTAFATDGPVLVDVVV-ASEELAM-PPQIKL 540
Cdd:PRK06276 483 QNLYYGKRQSEVHlgeTPDFVKLAESYGVKADRVEKPDEIKEALKEAIKSGEPYLLDIIIdPAEALPMvPPGGNL 557
|
|
| TPP_PYR_POX |
cd07039 |
Pyrimidine (PYR) binding domain of POX; Thiamine pyrophosphate (TPP family), pyrimidine (PYR) ... |
4-166 |
2.94e-78 |
|
Pyrimidine (PYR) binding domain of POX; Thiamine pyrophosphate (TPP family), pyrimidine (PYR) binding domain of pyruvate oxidase (POX) subfamily. The PYR domain is found in many key metabolic enzymes which use TPP (also known as thiamine diphosphate) as a cofactor. TPP binds in the cleft formed by a PYR domain and a PP domain. The PYR domain, binds the aminopyrimidine ring of TPP, the PP domain binds the diphosphate residue. The PYR and PP domains have a common fold, but do not share strong sequence conservation. The PP domain is not included in this sub-family. Most TPP-dependent enzymes have the PYR and PP domains on the same subunit although these domains can be alternatively arranged in the primary structure. TPP-dependent enzymes are multisubunit proteins, the smallest catalytic unit being a dimer-of-active sites. Lactobacillus plantarum POX is a homotetramer (dimer-of-homodimers), having two active sites per homodimer lying between PYR and PP domains of different subunits. POX decarboxylates pyruvate, producing hydrogen peroxide and the energy-storage metabolite acetylphosphate.
Pssm-ID: 132922 [Multi-domain] Cd Length: 164 Bit Score: 244.00 E-value: 2.94e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 4 TVAAYIAKTLEQAGVKRIWGVTGDSLNGLSDSLNRMGTIDWMPTRHEEVAAFAAGAEAQLTGELAVCAGSCGPGNLHLIN 83
Cdd:cd07039 1 TVADVIVETLENWGVKRVYGIPGDSINGLMDALRREGKIEFIQVRHEEAAAFAASAEAKLTGKLGVCLGSSGPGAIHLLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 84 GLFDCHRNHVPVLAIAAHIPSSEIGSGYFQETHPQELFRECSHYCELVSTPEQIPQVLAIAMRKAVINRGVSVVVLPGDV 163
Cdd:cd07039 81 GLYDAKRDRAPVLAIAGQVPTDELGTDYFQEVDLLALFKDVAVYNETVTSPEQLPELLDRAIRTAIAKRGVAVLILPGDV 160
|
...
gi 640683833 164 ALK 166
Cdd:cd07039 161 QDA 163
|
|
| PRK06048 |
PRK06048 |
acetolactate synthase large subunit; |
2-535 |
1.71e-77 |
|
acetolactate synthase large subunit;
Pssm-ID: 180368 [Multi-domain] Cd Length: 561 Bit Score: 255.08 E-value: 1.71e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 2 KQTVAAYIAKTLEQAGVKRIWGVTGDSLNGLSDSLNRMGtIDWMPTRHEEVAAFAAGAEAQLTGELAVCAGSCGPGNLHL 81
Cdd:PRK06048 7 KMTGARAIIKCLEKEGVEVIFGYPGGAIIPVYDELYDSD-LRHILVRHEQAAAHAADGYARATGKVGVCVATSGPGATNL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 82 INGLFDCHRNHVPVLAIAAHIPSSEIGSGYFQETHPQELFRECSHYCELVSTPEQIPQVLAIAMRKAVINRGVSVVV-LP 160
Cdd:PRK06048 86 VTGIATAYMDSVPIVALTGQVPRSMIGNDAFQEADITGITMPITKHNYLVQDAKDLPRIIKEAFHIASTGRPGPVLIdLP 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 161 GDVALKAA----PESASSHWYHaplPQVTPAEEELKKLAQLLRYSSNIALMCGSGC--AGAHKELVDFAAKLKAPIVHAL 234
Cdd:PRK06048 166 KDVTTAEIdfdyPDKVELRGYK---PTYKGNPQQIKRAAELIMKAERPIIYAGGGVisSNASEELVELAETIPAPVTTTL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 235 RGKEHVEYDNPYDVGMTGLIGFSSGFHTMMNADTLVLLGTQFPYR------AFYPtDAKIIQIDINPGSIGAHSKVDMAL 308
Cdd:PRK06048 243 MGIGAIPTEHPLSLGMLGMHGTKYANYAIQESDLIIAVGARFDDRvtgklaSFAP-NAKIIHIDIDPAEISKNVKVDVPI 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 309 VGDIKSTLSALMPHLEEKTDRKFLDKALEHyrdaRKGLDDLAKPSDKTIHPQYLAQRISHYADDdAIFTCDVGTPTVWAA 388
Cdd:PRK06048 322 VGDAKQVLKSLIKYVQYCDRKEWLDKINQW----KKEYPLKYKEREDVIKPQYVIEQIYELCPD-AIIVTEVGQHQMWAA 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 389 RYLQMNGKRRLLGSFNHGSMANAMPQAIGAKATAPDRQVVAMCGDGGFSMLMGDFLSLAQMKLPVKIVIFNNSVLGFVA- 467
Cdd:PRK06048 397 QYFKYKYPRTFITSGGLGTMGYGFPAAIGAKVGKPDKTVIDIAGDGSFQMNSQELATAVQNDIPVIVAILNNGYLGMVRq 476
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 640683833 468 -MEMKAGGYLTDGTELHATNFARIAEACGIKGIRVESASEVDEALQTAFATDGPVLVDVVVASEELAMP 535
Cdd:PRK06048 477 wQELFYDKRYSHTCIKGSVDFVKLAEAYGALGLRVEKPSEVRPAIEEAVASDRPVVIDFIVECEENVSP 545
|
|
| PRK08527 |
PRK08527 |
acetolactate synthase large subunit; |
1-535 |
1.47e-71 |
|
acetolactate synthase large subunit;
Pssm-ID: 181458 [Multi-domain] Cd Length: 563 Bit Score: 239.62 E-value: 1.47e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 1 MKQTVAAYIAKTLEQAGVKRIWGVTGDSLNGLSDSLNRMGTIDWMPTRHEEVAAFAAGAEAQLTGELAVCAGSCGPGNLH 80
Cdd:PRK08527 1 KKLSGSQMVCEALKEEGVKVVFGYPGGAILNIYDEIYKQNYFKHILTRHEQAAVHAADGYARASGKVGVAIVTSGPGFTN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 81 LINGLFDCHRNHVPVLAIAAHIPSSEIGSGYFQETHPQELFRECSHYCELVSTPEQIPQVLAIAMRKAVINRGVSVVV-L 159
Cdd:PRK08527 81 AVTGLATAYMDSIPLVLISGQVPNSLIGTDAFQEIDAVGISRPCVKHNYLVKSIEELPRILKEAFYIARSGRPGPVHIdI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 160 PGDVALKAA----PESASSHWYHaplPQVTPAEEELKKLAQLLRYSSNIALMCGSGC--AGAHKELVDFAAKLKAPIVHA 233
Cdd:PRK08527 161 PKDVTATLGefeyPKEISLKTYK---PTYKGNSRQIKKAAEAIKEAKKPLFYLGGGAilSNASEEIRELVKKTGIPAVET 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 234 LRGKEHVEYDNPYDVGMTGLIGFSSGFHTMMNADTLVLLGTQFPYRAFYPTD-----AKIIQIDINPGSIGAHSKVDMAL 308
Cdd:PRK08527 238 LMARGVLRSDDPLLLGMLGMHGSYAANMAMSECDLLISLGARFDDRVTGKLSefakhAKIIHVDIDPSSISKIVNADYPI 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 309 VGDIKSTLSALMPHLEEKTDRKFlDKALEHYRDARKgLDDLA-KPSDKTIHPQYLAQRISHYADDDAIFTCDVGTPTVWA 387
Cdd:PRK08527 318 VGDLKNVLKEMLEELKEENPTTY-KEWREILKRYNE-LHPLSyEDSDEVLKPQWVIERVGELLGDDAIISTDVGQHQMWV 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 388 ARYLQMNGKRRLLGSFNHGSMANAMPQAIGAKATAPDRQVVAMCGDGGFSMLMGDFLSLAQMKLPVKIVIFNNSVLGFVA 467
Cdd:PRK08527 396 AQFYPFNYPRQLATSGGLGTMGYGLPAALGAKLAVPDKVVINFTGDGSILMNIQELMTAVEYKIPVINIILNNNFLGMVR 475
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 640683833 468 --MEMKAGGYLTDgTELHAT-NFARIAEACGIKGIRVESASEVDEALQTAFATDGPVLVDVVVASEELAMP 535
Cdd:PRK08527 476 qwQTFFYEERYSE-TDLSTQpDFVKLAESFGGIGFRVTTKEEFDKALKEALESDKVALIDVKIDRFENVLP 545
|
|
| PRK08155 |
PRK08155 |
acetolactate synthase large subunit; |
1-535 |
9.70e-68 |
|
acetolactate synthase large subunit;
Pssm-ID: 181257 [Multi-domain] Cd Length: 564 Bit Score: 229.59 E-value: 9.70e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 1 MKQTVAAYIAKTLEQAGVKRIWGVTGDSLNGLSDSLNRMGTIDWMPTRHEEVAAFAAGAEAQLTGELAVCAGSCGPGNLH 80
Cdd:PRK08155 11 KRFTGAELIVRLLERQGIRIVTGIPGGAILPLYDALSQSTQIRHILARHEQGAGFIAQGMARTTGKPAVCMACSGPGATN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 81 LINGLFDCHRNHVPVLAIAAHIPSSEIGSGYFQETHPQELFRECSHYCELVSTPEQIPQVLAIAMRKAVINRGVSVVV-L 159
Cdd:PRK08155 91 LVTAIADARLDSIPLVCITGQVPASMIGTDAFQEVDTYGISIPITKHNYLVRDIEELPQVISDAFRIAQSGRPGPVWIdI 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 160 PGDV-----ALKAAPESAsshwyhAPLPQVTPAEEELKKLAQLLRYSSNIALMCGSG--CAGAHKELVDFAAKLKAPIVH 232
Cdd:PRK08155 171 PKDVqtaviELEALPAPA------EKDAAPAFDEESIRDAAAMINAAKRPVLYLGGGviNSGAPARARELAEKAQLPTTM 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 233 ALRGKEHVEYDNPYDVGMTGLIGFSSGFHTMMNADTLVLLGTQFPYRA------FYPtDAKIIQIDINPGSIGAHSKVDM 306
Cdd:PRK08155 245 TLMALGMLPKAHPLSLGMLGMHGARSTNYILQEADLLIVLGARFDDRAigkteqFCP-NAKIIHVDIDRAELGKIKQPHV 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 307 ALVGDIKSTLSALMPHLeEKTDRKfldKALEHYRDARKGLDDLAKPSDKTIHPQYLAQRISHYADDDAIFTCDVGTPTVW 386
Cdd:PRK08155 324 AIQADVDDVLAQLLPLV-EAQPRA---EWHQLVADLQREFPCPIPKADDPLSHYGLINAVAACVDDNAIITTDVGQHQMW 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 387 AARYLQMNGKRRLLGSFNHGSMANAMPQAIGAKATAPDRQVVAMCGDGGFSMLMGDFLSLAQMKLPVKIVIFNNSVLGFV 466
Cdd:PRK08155 400 TAQAYPLNRPRQWLTSGGLGTMGFGLPAAIGAALANPERKVLCFSGDGSLMMNIQEMATAAENQLDVKIILMNNEALGLV 479
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 640683833 467 --AMEMKAGGYLTDGTELHATNFARIAEACGIKGIRVESASEVDEALQTAFATDGPVLVDVVVASEELAMP 535
Cdd:PRK08155 480 hqQQSLFYGQRVFAATYPGKINFMQIAAGFGLETCDLNNEADPQAALQEAINRPGPALIHVRIDAEEKVYP 550
|
|
| PRK07282 |
PRK07282 |
acetolactate synthase large subunit; |
9-535 |
8.37e-67 |
|
acetolactate synthase large subunit;
Pssm-ID: 180919 [Multi-domain] Cd Length: 566 Bit Score: 227.01 E-value: 8.37e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 9 IAKTLEQAGVKRIWGVTGDSLNGLSDSLNRMGTIDWMPTRHEEVAAFAAGAEAQLTGELAVCAGSCGPGNLHLINGLFDC 88
Cdd:PRK07282 16 VLETLRDLGVDTIFGYPGGAVLPLYDAIYNFEGIRHILARHEQGALHEAEGYAKSTGKLGVAVVTSGPGATNAITGIADA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 89 HRNHVPVLAIAAHIPSSEIGSGYFQETHPQELFRECSHYCELVSTPEQIPQVLAIAMRKAVINRGVSVVV-LPGDVALKA 167
Cdd:PRK07282 96 MSDSVPLLVFTGQVARAGIGKDAFQEADIVGITMPITKYNYQIRETADIPRIITEAVHIATTGRPGPVVIdLPKDVSALE 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 168 APESASSHwYHAP--LPQVTPAEEELKKLAQLLRYSSNIALMCGSGC--AGAHKELVDFAAKLKAPIVHALRGKEHVEYD 243
Cdd:PRK07282 176 TDFIYDPE-VNLPsyQPTLEPNDMQIKKILKQLSKAKKPVILAGGGInyAEAATELNAFAERYQIPVVTTLLGQGTIATS 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 244 NPYDVGMTGLIGFSSGFHTMMNADTLVLLGTQFPYR-----AFYPTDAKIIQIDINPGSIGAHSKVDMALVGDIKSTLSA 318
Cdd:PRK07282 255 HPLFLGMGGMHGSYAANIAMTEADFMINIGSRFDDRltgnpKTFAKNAKVAHIDIDPAEIGKIIKTDIPVVGDAKKALQM 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 319 LMPHLEEKTD-RKFLDKALEHYRDARKglddlAKPSDKTIHPQYLAQRISHYADDDAIFTCDVGTPTVWAARYLQMNGKR 397
Cdd:PRK07282 335 LLAEPTVHNNtEKWIEKVTKDKNRVRS-----YDKKERVVQPQAVIERIGELTNGDAIVVTDVGQHQMWAAQYYPYQNER 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 398 RLLGSFNHGSMANAMPQAIGAKATAPDRQVVAMCGDGGFSMLMGDFLSLAQMKLPVKIVIFNNSVLGFVAMEMKAggyLT 477
Cdd:PRK07282 410 QLVTSGGLGTMGFGIPAAIGAKIANPDKEVILFVGDGGFQMTNQELAILNIYKVPIKVVMLNNHSLGMVRQWQES---FY 486
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 640683833 478 DGTELHAT-----NFARIAEACGIKGIRVESASEVDEALQTaFATDGPVLVDVVVASEELAMP 535
Cdd:PRK07282 487 EGRTSESVfdtlpDFQLMAQAYGIKHYKFDNPETLAQDLEV-ITEDVPMLIEVDISRKEHVLP 548
|
|
| PRK07418 |
PRK07418 |
acetolactate synthase large subunit; |
1-531 |
1.07e-66 |
|
acetolactate synthase large subunit;
Pssm-ID: 236014 [Multi-domain] Cd Length: 616 Bit Score: 228.01 E-value: 1.07e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 1 MKQTVAAYIAKTLEQAGVKRIWGVTGDSLNGLSDSLNRM---GTIDWMPTRHEEVAAFAAGAEAQLTGELAVCAGSCGPG 77
Cdd:PRK07418 17 QRATGAYALMDSLKRHGVKHIFGYPGGAILPIYDELYKAeaeGWLKHILVRHEQGAAHAADGYARATGKVGVCFGTSGPG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 78 NLHLINGLFDCHRNHVPVLAIAAHIPSSEIGSGYFQETHPQELFRECSHYCELVSTPEQIPQVLAIAMRKAVINRGVSVV 157
Cdd:PRK07418 97 ATNLVTGIATAQMDSVPMVVITGQVPRPAIGTDAFQETDIFGITLPIVKHSYVVRDPSDMARIVAEAFHIASSGRPGPVL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 158 V-LPGDVALK------AAPESASSHWYHaplPQVTPAEEELKKLAQLLRYSSNIALMCGSGC--AGAHKELVDFAAKLKA 228
Cdd:PRK07418 177 IdIPKDVGQEefdyvpVEPGSVKPPGYR---PTVKGNPRQINAALKLIEEAERPLLYVGGGAisAGAHAELKELAERFQI 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 229 PIVHALRGKEHVEYDNPYDVGMTGLIGFSSGFHTMMNADTLVLLGTQFPYRA------FYPTdAKIIQIDINPGSIGAHS 302
Cdd:PRK07418 254 PVTTTLMGKGAFDEHHPLSVGMLGMHGTAYANFAVTECDLLIAVGARFDDRVtgkldeFASR-AKVIHIDIDPAEVGKNR 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 303 KVDMALVGDIKSTLSALMPHLEEKTDRKFLDKALEHYRDARKGLDDLAKPSDKTIHPQYLAQRISHYAdDDAIFTCDVGT 382
Cdd:PRK07418 333 RPDVPIVGDVRKVLVKLLERSLEPTTPPRTQAWLERINRWKQDYPLVVPPYEGEIYPQEVLLAVRDLA-PDAYYTTDVGQ 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 383 PTVWAARYLQmNGKRRLLGSFNHGSMANAMPQAIGAKATAPDRQVVAMCGDGGFSMLMGDFLSLAQMKLPVKIVIFNNSV 462
Cdd:PRK07418 412 HQMWAAQFLR-NGPRRWISSAGLGTMGFGMPAAMGVKVALPDEEVICIAGDASFLMNIQELGTLAQYGINVKTVIINNGW 490
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 463 LGFV-------------AMEMKAGgyltdgtelhATNFARIAEACGIKGIRVESASEVDEALQTAFATDGPVLVDVVVAS 529
Cdd:PRK07418 491 QGMVrqwqesfygerysASNMEPG----------MPDFVKLAEAFGVKGMVISERDQLKDAIAEALAHDGPVLIDVHVRR 560
|
..
gi 640683833 530 EE 531
Cdd:PRK07418 561 DE 562
|
|
| PRK07789 |
PRK07789 |
acetolactate synthase 1 catalytic subunit; Validated |
4-527 |
1.89e-66 |
|
acetolactate synthase 1 catalytic subunit; Validated
Pssm-ID: 236098 [Multi-domain] Cd Length: 612 Bit Score: 227.17 E-value: 1.89e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 4 TVAAYIAKTLEQAGVKRIWGVTGDSLNGLSDSLNRMGTIDWMPTRHEEVAAFAAGAEAQLTGELAVCAGSCGPGNLHLIN 83
Cdd:PRK07789 32 TGAQAVVRSLEELGVDVVFGIPGGAILPVYDPLFDSTKVRHVLVRHEQGAGHAAEGYAQATGRVGVCMATSGPGATNLVT 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 84 GLFDCHRNHVPVLAIAAHIPSSEIGSGYFQE------THPqelfreCSHYCELVSTPEQIPQVLAIAMRKAVINRGVSVV 157
Cdd:PRK07789 112 PIADANMDSVPVVAITGQVGRGLIGTDAFQEadivgiTMP------ITKHNFLVTDADDIPRVIAEAFHIASTGRPGPVL 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 158 VlpgDVALKAAPESASSHW--------YHaplPQVTPAEEELKKLAQLLRYSSNIALMCGSGC--AGAHKELVDFAAKLK 227
Cdd:PRK07789 186 V---DIPKDALQAQTTFSWpprmdlpgYR---PVTKPHGKQIREAAKLIAAARRPVLYVGGGVirAEASAELRELAELTG 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 228 APIVHALRGKEHVEYDNPYDVGMTGLIGFSSGFHTMMNADTLVLLGTQFPYR------AFYPtDAKIIQIDINPGSIGAH 301
Cdd:PRK07789 260 IPVVTTLMARGAFPDSHPQHLGMPGMHGTVAAVAALQRSDLLIALGARFDDRvtgkldSFAP-DAKVIHADIDPAEIGKN 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 302 SKVDMALVGDIKSTLSALMPHLEektdRKFLDKALEHYRDARKGLDDL--------AKPSDKTIHPQYLAQRISHYADDD 373
Cdd:PRK07789 339 RHADVPIVGDVKEVIAELIAALR----AEHAAGGKPDLTAWWAYLDGWretyplgyDEPSDGSLAPQYVIERLGEIAGPD 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 374 AIFTCDVGTPTVWAARYLQMNGKRRLLGSFNHGSMANAMPQAIGAKATAPDRQVVAMCGDGGFSMLMGDFLSLAQMKLPV 453
Cdd:PRK07789 415 AIYVAGVGQHQMWAAQFIDYEKPRTWLNSGGLGTMGYAVPAAMGAKVGRPDKEVWAIDGDGCFQMTNQELATCAIEGIPI 494
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 454 KIVIFNNSVLGFVAMEMK---AGGYltDGTELHA-----TNFARIAEACGIKGIRVESASEVDEALQTAFAT-DGPVLVD 524
Cdd:PRK07789 495 KVALINNGNLGMVRQWQTlfyEERY--SNTDLHThshriPDFVKLAEAYGCVGLRCEREEDVDAVIEKARAInDRPVVID 572
|
...
gi 640683833 525 VVV 527
Cdd:PRK07789 573 FVV 575
|
|
| PRK06725 |
PRK06725 |
acetolactate synthase large subunit; |
4-535 |
2.82e-66 |
|
acetolactate synthase large subunit;
Pssm-ID: 180672 [Multi-domain] Cd Length: 570 Bit Score: 225.62 E-value: 2.82e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 4 TVAAYIAKTLEQAGVKRIWGVTGDSLNGLSDSLNRMGtIDWMPTRHEEVAAFAAGAEAQLTGELAVCAGSCGPGNLHLIN 83
Cdd:PRK06725 16 TGAGHVIQCLKKLGVTTVFGYPGGAILPVYDALYESG-LKHILTRHEQAAIHAAEGYARASGKVGVVFATSGPGATNLVT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 84 GLFDCHRNHVPVLAIAAHIPSSEIGSGYFQETHPQELFRECSHYCELVSTPEQIPQVLAIAMRKAVINR-GVSVVVLPGD 162
Cdd:PRK06725 95 GLADAYMDSIPLVVITGQVATPLIGKDGFQEADVVGITVPVTKHNYQVRDVNQLSRIVQEAFYIAESGRpGPVLIDIPKD 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 163 VALKAA----PESASSHWYHaplPQVTPAEEELKKLAQLLRYSSNIALMCGSGC--AGAHKELVDFAAKLKAPIVHALRG 236
Cdd:PRK06725 175 VQNEKVtsfyNEVVEIPGYK---PEPRPDSMKLREVAKAISKAKRPLLYIGGGVihSGGSEELIEFARENRIPVVSTLMG 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 237 KEHVEYDNPYDVGMTGLIGFSSGFHTMMNADTLVLLGTQFPYRA------FYPtDAKIIQIDINPGSIGAHSKVDMALVG 310
Cdd:PRK06725 252 LGAYPPGDPLFLGMLGMHGTYAANMAVTECDLLLALGVRFDDRVtgklelFSP-HSKKVHIDIDPSEFHKNVAVEYPVVG 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 311 DIKSTLSALMPHLEEKTDRKFLDKALEHyrDARKGLDDLAKPSDktIHPQYLAQRISHYADDDAIFTCDVGTPTVWAARY 390
Cdd:PRK06725 331 DVKKALHMLLHMSIHTQTDEWLQKVKTW--KEEYPLSYKQKESE--LKPQHVINLVSELTNGEAIVTTEVGQHQMWAAHF 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 391 LQMNGKRRLLGSFNHGSMANAMPQAIGAKATAPDRQVVAMCGDGGFSMLMGDFLSLAQMKLPVKIVIFNNSVLGFVA--M 468
Cdd:PRK06725 407 YKAKNPRTFLTSGGLGTMGFGFPAAIGAQLAKEEELVICIAGDASFQMNIQELQTIAENNIPVKVFIINNKFLGMVRqwQ 486
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 640683833 469 EMKAGGYLTDgTELHATNFARIAEACGIKGIRVESASEVDEALQTAFATDGPVLVDVVVASEELAMP 535
Cdd:PRK06725 487 EMFYENRLSE-SKIGSPDFVKVAEAYGVKGLRATNSTEAKQVMLEAFAHEGPVVVDFCVEEGENVFP 552
|
|
| PRK07710 |
PRK07710 |
acetolactate synthase large subunit; |
6-535 |
2.64e-65 |
|
acetolactate synthase large subunit;
Pssm-ID: 236076 [Multi-domain] Cd Length: 571 Bit Score: 223.10 E-value: 2.64e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 6 AAYIAKTLEQAGVKRIWGVTGDSLNGLSDSLNRMGTIDWMpTRHEEVAAFAAGAEAQLTGELAVCAGSCGPGNLHLINGL 85
Cdd:PRK07710 19 AQMLIEALEKEGVEVIFGYPGGAVLPLYDALYDCGIPHIL-TRHEQGAIHAAEGYARISGKPGVVIATSGPGATNVVTGL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 86 FDCHRNHVPVLAIAAHIPSSEIGSGYFQETHPQELFRECSHYCELVSTPEQIPQVLAIAMRKAVINRGVSVVV-LPGDVA 164
Cdd:PRK07710 98 ADAMIDSLPLVVFTGQVATSVIGSDAFQEADIMGITMPVTKHNYQVRKASDLPRIIKEAFHIATTGRPGPVLIdIPKDMV 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 165 LkAAPESASSHWYHAP--LPQVTPAEEELKKLAQLLRYSSNIALMCGSGC--AGAHKELVDFAAKLKAPIVHALRGKEHV 240
Cdd:PRK07710 178 V-EEGEFCYDVQMDLPgyQPNYEPNLLQIRKLVQAVSVAKKPVILAGAGVlhAKASKELTSYAEQQEIPVVHTLLGLGGF 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 241 EYDNPYDVGMTGLIGFSSGFHTMMNADTLVLLGTQFPYR-----AFYPTDAKIIQIDINPGSIGAHSKVDMALVGDIKST 315
Cdd:PRK07710 257 PADHPLFLGMAGMHGTYTANMALYECDLLINIGARFDDRvtgnlAYFAKEATVAHIDIDPAEIGKNVPTEIPIVADAKQA 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 316 LSALMPHLEEKTDRKFLDKALehyrDARKGLDDLA-KPSDKTIHPQYLAQRISHYADDDAIFTCDVGTPTVWAARYLQMN 394
Cdd:PRK07710 337 LQVLLQQEGKKENHHEWLSLL----KNWKEKYPLSyKRNSESIKPQKAIEMLYEITKGEAIVTTDVGQHQMWAAQYYPFK 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 395 GKRRLLGSFNHGSMANAMPQAIGAKATAPDRQVVAMCGDGGFSMLMGDFLSLAQMKLPVKIVIFNNSVLGFVAM--EMKA 472
Cdd:PRK07710 413 TPDKWVTSGGLGTMGFGLPAAIGAQLAKPDETVVAIVGDGGFQMTLQELSVIKELSLPVKVVILNNEALGMVRQwqEEFY 492
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 640683833 473 GGYLTDGTELHATNFARIAEACGIKGIRVESASEVDEALQTAFATDGPVLVDVVVASEELAMP 535
Cdd:PRK07710 493 NQRYSHSLLSCQPDFVKLAEAYGIKGVRIDDELEAKEQLQHAIELQEPVVIDCRVLQSEKVMP 555
|
|
| ilvB |
CHL00099 |
acetohydroxyacid synthase large subunit |
1-531 |
6.68e-64 |
|
acetohydroxyacid synthase large subunit
Pssm-ID: 214363 [Multi-domain] Cd Length: 585 Bit Score: 219.57 E-value: 6.68e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 1 MKQTVAAYIAKTLEQAGVKRIWGVTGDSLNGLSDSL---NRMGTIDWMPTRHEEVAAFAAGAEAQLTGELAVCAGSCGPG 77
Cdd:CHL00099 8 REKTGAFALIDSLVRHGVKHIFGYPGGAILPIYDELyawEKKGLIKHILVRHEQGAAHAADGYARSTGKVGVCFATSGPG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 78 NLHLINGLFDCHRNHVPVLAIAAHIPSSEIGSGYFQETHPQELFRECSHYCELVSTPEQIPQVLAIAMRKAVINRGVSVV 157
Cdd:CHL00099 88 ATNLVTGIATAQMDSVPLLVITGQVGRAFIGTDAFQEVDIFGITLPIVKHSYVVRDARDISRIVAEAFYIAKHGRPGPVL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 158 V-LPGDVALKAAPesasshwYHAPLPQ------------VTPAEEELKKLAQLLRYSSNIALMCGSGC--AGAHKELVDF 222
Cdd:CHL00099 168 IdIPKDVGLEKFD-------YYPPEPGntiikilgcrpiYKPTIKRIEQAAKLILQSSQPLLYVGGGAiiSDAHQEITEL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 223 AAKLKAPIVHALRGKEHVEYDNPYDVGMTGLIGFSSGFHTMMNADTLVLLGTQFPYRAF-----YPTDAKIIQIDINPGS 297
Cdd:CHL00099 241 AELYKIPVTTTLMGKGIFDEDHPLCLGMLGMHGTAYANFAVSECDLLIALGARFDDRVTgkldeFACNAQVIHIDIDPAE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 298 IGAHSKVDMALVGDIKSTLSALMPHLeeKTDRKFLDKalEHYRDARKGLDD-------LAKPSDKTIHPQYLAQRISHYA 370
Cdd:CHL00099 321 IGKNRIPQVAIVGDVKKVLQELLELL--KNSPNLLES--EQTQAWRERINRwrkeyplLIPKPSTSLSPQEVINEISQLA 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 371 DDdAIFTCDVGTPTVWAARYLQMnGKRRLLGSFNHGSMANAMPQAIGAKATAPDRQVVAMCGDGGFSMLMGDFLSLAQMK 450
Cdd:CHL00099 397 PD-AYFTTDVGQHQMWAAQFLKC-KPRKWLSSAGLGTMGYGLPAAIGAQIAHPNELVICISGDASFQMNLQELGTIAQYN 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 451 LPVKIVIFNNSVLGFVAM-------EMKAGGYLTDGtelhATNFARIAEACGIKGIRVESASEVDEALQTAFATDGPVLV 523
Cdd:CHL00099 475 LPIKIIIINNKWQGMVRQwqqafygERYSHSNMEEG----APDFVKLAEAYGIKGLRIKSRKDLKSSLKEALDYDGPVLI 550
|
....*...
gi 640683833 524 DVVVASEE 531
Cdd:CHL00099 551 DCQVIEDE 558
|
|
| PRK08979 |
PRK08979 |
acetolactate synthase 3 large subunit; |
6-539 |
1.53e-63 |
|
acetolactate synthase 3 large subunit;
Pssm-ID: 181602 [Multi-domain] Cd Length: 572 Bit Score: 218.54 E-value: 1.53e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 6 AAYIAKTLEQAGVKRIWGVTGDSLNGLSDSLNRMGTIDWMPTRHEEVAAFAAGAEAQLTGELAVCAGSCGPGNLHLINGL 85
Cdd:PRK08979 7 ASMIVRSLIDEGVKHIFGYPGGSVLDIYDALHEKSGIEHILVRHEQAAVHMADGYARATGKVGVVLVTSGPGATNTITGI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 86 FDCHRNHVPVLAIAAHIPSSEIGSGYFQETHPQELFRECSHYCELVSTPEQIPQVLAIAMRKAVINR-GVSVVVLPGDV- 163
Cdd:PRK08979 87 ATAYMDSIPMVVLSGQVPSNLIGNDAFQECDMIGISRPVVKHSFLVKDAEDIPEIIKKAFYIASTGRpGPVVIDLPKDCl 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 164 --ALK---AAPESASSHWYHaplPQVTPAEEELKKLAQLLRYSSNIALMCGSGC--AGAHKELVDFAAKLKAPIVHALRG 236
Cdd:PRK08979 167 npAILhpyEYPESIKMRSYN---PTTSGHKGQIKRGLQALLAAKKPVLYVGGGAiiSGADKQILQLAEKLNLPVVSTLMG 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 237 KEHVEYDNPYDVGMTGLIGFSSGFHTMMNADTLVLLGTQFPYRAF-----YPTDAKIIQIDINPGSIGAHSKVDMALVGD 311
Cdd:PRK08979 244 LGAFPGTHKNSLGMLGMHGRYEANMAMHNADLIFGIGVRFDDRTTnnlekYCPNATILHIDIDPSSISKTVRVDIPIVGS 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 312 IKSTLSALMPHLEEKTDRKflDKA--------LEHYRDaRKGLDdLAKPSDKtIHPQYLAQRISHYADDDAIFTCDVGTP 383
Cdd:PRK08979 324 ADKVLDSMLALLDESGETN--DEAaiaswwneIEVWRS-RNCLA-YDKSSER-IKPQQVIETLYKLTNGDAYVASDVGQH 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 384 TVWAARYLQMNGKRRLLGSFNHGSMANAMPQAIGAKATAPDRQVVAMCGDGGFSMLMGDFLSLAQMKLPVKIVIFNNSVL 463
Cdd:PRK08979 399 QMFAALYYPFDKPRRWINSGGLGTMGFGLPAAMGVKFAMPDETVVCVTGDGSIQMNIQELSTALQYDIPVKIINLNNRFL 478
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 640683833 464 GFVA--MEMKAGGYLTDGTELHATNFARIAEACGIKGIRVESASEVDEALQTAFA-TDGPVLVDVVVASEELAMPPQIK 539
Cdd:PRK08979 479 GMVKqwQDMIYQGRHSHSYMDSVPDFAKIAEAYGHVGIRISDPDELESGLEKALAmKDRLVFVDINVDETEHVYPMQIR 557
|
|
| PLN02470 |
PLN02470 |
acetolactate synthase |
13-535 |
1.55e-62 |
|
acetolactate synthase
Pssm-ID: 215261 [Multi-domain] Cd Length: 585 Bit Score: 216.14 E-value: 1.55e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 13 LEQAGVKRIWGVTGDSLNGLSDSLNRMGTIDWMPTRHEEVAAFAAGAEAQLTGELAVCAGSCGPGNLHLINGLFDCHRNH 92
Cdd:PLN02470 23 LEREGVDTVFAYPGGASMEIHQALTRSNCIRNVLCRHEQGEVFAAEGYAKASGKVGVCIATSGPGATNLVTGLADALLDS 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 93 VPVLAIAAHIPSSEIGSGYFQETHPQELFRECSHYCELVSTPEQIPQVLAIAMRKAVINRGVSVVV-LPGDVALK-AAP- 169
Cdd:PLN02470 103 VPLVAITGQVPRRMIGTDAFQETPIVEVTRSITKHNYLVMDVEDIPRVIREAFFLASSGRPGPVLVdIPKDIQQQlAVPn 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 170 --ESASSHWYHAPLPQVtPAEEELKKLAQLLRYSSNIALMCGSGCAGAHKELVDFAAKLKAPIVHALRGKEHVEYDNPYD 247
Cdd:PLN02470 183 wnQPMKLPGYLSRLPKP-PEKSQLEQIVRLISESKRPVVYVGGGCLNSSEELREFVELTGIPVASTLMGLGAFPASDELS 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 248 VGMTGLIGFSSGFHTMMNADTLVLLGTQFPYR------AFyPTDAKIIQIDINPGSIGAHSKVDMALVGDIKSTLSALMP 321
Cdd:PLN02470 262 LQMLGMHGTVYANYAVDSADLLLAFGVRFDDRvtgkleAF-ASRASIVHIDIDPAEIGKNKQPHVSVCADVKLALQGLNK 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 322 HLEEKTDRKFLDKALEHYRDARKGLDDLAKPS-DKTIHPQYLAQRISHYADDDAIFTCDVGTPTVWAARYLQMNGKRRLL 400
Cdd:PLN02470 341 LLEERKAKRPDFSAWRAELDEQKEKFPLSYPTfGDAIPPQYAIQVLDELTDGNAIISTGVGQHQMWAAQWYKYKEPRRWL 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 401 GSFNHGSMANAMPQAIGAKATAPDRQVVAMCGDGGFSMLMGDFLSLAQMKLPVKIVIFNNSVLGFVAM-------EMKAG 473
Cdd:PLN02470 421 TSGGLGAMGFGLPAAIGAAAANPDAIVVDIDGDGSFIMNIQELATIHVENLPVKIMVLNNQHLGMVVQwedrfykANRAH 500
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 640683833 474 GYLTD-GTELHA-TNFARIAEACGIKGIRVESASEVDEALQTAFATDGPVLVDVVVASEELAMP 535
Cdd:PLN02470 501 TYLGDpDAEAEIfPDFLKFAEGCKIPAARVTRKSDLREAIQKMLDTPGPYLLDVIVPHQEHVLP 564
|
|
| sulphoacet_xsc |
TIGR03457 |
sulfoacetaldehyde acetyltransferase; Members of this protein family are sulfoacetaldehyde ... |
2-535 |
3.61e-62 |
|
sulfoacetaldehyde acetyltransferase; Members of this protein family are sulfoacetaldehyde acetyltransferase, an enzyme of taurine utilization. Taurine, or 2-aminoethanesulfonate, can be used by bacteria as a source of carbon, nitrogen, and sulfur. [Central intermediary metabolism, Other]
Pssm-ID: 132497 [Multi-domain] Cd Length: 579 Bit Score: 214.73 E-value: 3.61e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 2 KQTVAAYIAKTLEQAGVKRIWGVTGDSLNGLSDSLNRMGtIDWMPTRHEEVAAFAAGAEAQLTGELAVCAGSCGPGNLHL 81
Cdd:TIGR03457 1 KMTPSEAFVEVLVANGVTHAFGIMGSAFMDAMDLFPPAG-IRFIPVVHEQGAGHMADGFARVTGRMSMVIGQNGPGVTNC 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 82 INGLFDCHRNHVPVLAIAAHIPSSEIGSGYFQETHPQELFRECSHYCELVSTPEQIPQVLAIAMRKAVINRGVSVVVLPG 161
Cdd:TIGR03457 80 VTAIAAAYWAHTPVVIVTPEAGTKTIGLGGFQEADQLPMFQEFTKYQGHVRHPSRMAEVLNRCFERAWREMGPAQLNIPR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 162 DvalkaapesassHWY---HAPLPQVTP------AEEELKKLAQLLRYSSNIALMCGSGC--AGAHKELVDFAAKLKAPI 230
Cdd:TIGR03457 160 D------------YFYgeiDVEIPRPVRldrgagGATSLAQAARLLAEAKFPVIISGGGVvmGDAVEECKALAERLGAPV 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 231 VHALRGKEHVEYDNPYDVGMTGLIGFSSGFHTMMNADTLVLLGTQF-PYRA-------FYPTDAKIIQIDINPGSIGAHS 302
Cdd:TIGR03457 228 VNSYLHNDSFPASHPLWVGPLGYQGSKAAMKLISDADVVLALGTRLgPFGTlpqygidYWPKNAKIIQVDANAKMIGLVK 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 303 KVDMALVGDIKSTLSALMPHLEEKT-DRKFLDKA--LEHYRDA-RKGLDDLAKPSDKT---------------IHPQYLA 363
Cdd:TIGR03457 308 KVTVGICGDAKAAAAEILQRLAGKAgDANRAERKakIQAERSAwEQELSEMTHERDPFsldmiveqrqeegnwLHPRQVL 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 364 QRISHYADDDAIFTCDVGTPTVWAARYLQMNGKRRLLGSFNHGSMANAMPQAIGAKATAPDRQVVAMCGDGGFSMLMGDF 443
Cdd:TIGR03457 388 RELEKAMPEDAIVSTDIGNINSVANSYLRFEKPRKFLAPMSFGNCGYAFPTIIGAKIAAPDRPVVAYAGDGAWGMSMNEI 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 444 LSLAQMKLPVKIVIFNNSVLGfvaMEMKAGGYLTD----GTELHA-TNFARIAEACGIKGIRVESASEVDEALQTAFA-- 516
Cdd:TIGR03457 468 MTAVRHDIPVTAVVFRNRQWG---AEKKNQVDFYNnrfvGTELESeLSFAGIADAMGAKGVVVDKPEDVGPALKKAIAaq 544
|
570
....*....|....*....
gi 640683833 517 TDGPVLVDVVVASEELAMP 535
Cdd:TIGR03457 545 AEGKTTVIEIVCTRELGDP 563
|
|
| PRK06965 |
PRK06965 |
acetolactate synthase 3 catalytic subunit; Validated |
6-525 |
2.50e-61 |
|
acetolactate synthase 3 catalytic subunit; Validated
Pssm-ID: 180780 [Multi-domain] Cd Length: 587 Bit Score: 212.74 E-value: 2.50e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 6 AAYIAKTLEQAGVKRIWGVTGDSLNGLSDSLNRMGTIDWMPTRHEEVAAFAAGAEAQLTGELAVCAGSCGPGNLHLINGL 85
Cdd:PRK06965 24 AEILMKALAAEGVEFIWGYPGGAVLYIYDELYKQDKIQHVLVRHEQAAVHAADGYARATGKVGVALVTSGPGVTNAVTGI 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 86 FDCHRNHVPVLAIAAHIPSSEIGSGYFQETHPQELFRECSHYCELVSTPEQipqvLAIAMRKAV-INR----GVSVVVLP 160
Cdd:PRK06965 104 ATAYMDSIPMVVISGQVPTAAIGQDAFQECDTVGITRPIVKHNFLVKDVRD----LAETVKKAFyIARtgrpGPVVVDIP 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 161 GDVALKAAPesasshwYHAP----LPQVTPAEE----ELKKLAQLLRYSSNIALMCGSGC--AGAHKELVDFAAKLKAPI 230
Cdd:PRK06965 180 KDVSKTPCE-------YEYPksveMRSYNPVTKghsgQIRKAVSLLLSAKRPYIYTGGGVilANASRELRQLADLLGYPV 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 231 VHALRGKEHVEYDNPYDVGMTGLIGFSSGFHTMMNADTLVLLGTQFPYRA------FYPTDAKIIQIDINPGSIGAHSKV 304
Cdd:PRK06965 253 TNTLMGLGAYPASDKKFLGMLGMHGTYEANMAMQHCDVLIAIGARFDDRVignpahFASRPRKIIHIDIDPSSISKRVKV 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 305 DMALVGDIKSTLSALMPHLEE---KTDRKFLDKALEHYRDARKgLDDLA-KPSDKTIHPQYLAQRISHYADDDAIFTCDV 380
Cdd:PRK06965 333 DIPIVGDVKEVLKELIEQLQTaehGPDADALAQWWKQIEGWRS-RDCLKyDRESEIIKPQYVVEKLWELTDGDAFVCSDV 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 381 GTPTVWAARYLQMNGKRRLLGSFNHGSMANAMPQAIGAKATAPDRQVVAMCGDGGFSMLMGDFLSLAQMKLPVKIVIFNN 460
Cdd:PRK06965 412 GQHQMWAAQFYRFNEPRRWINSGGLGTMGVGLPYAMGIKMAHPDDDVVCITGEGSIQMCIQELSTCLQYDTPVKIISLNN 491
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 640683833 461 SVLGFVA--MEMKAGGYLTDGTELHATNFARIAEACGIKGIRVESASEVDEALQTAFA-TDGPVLVDV 525
Cdd:PRK06965 492 RYLGMVRqwQEIEYSKRYSHSYMDALPDFVKLAEAYGHVGMRIEKTSDVEPALREALRlKDRTVFLDF 559
|
|
| PRK08978 |
PRK08978 |
acetolactate synthase 2 catalytic subunit; Reviewed |
64-531 |
1.28e-60 |
|
acetolactate synthase 2 catalytic subunit; Reviewed
Pssm-ID: 181601 [Multi-domain] Cd Length: 548 Bit Score: 210.12 E-value: 1.28e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 64 TGELAVCAGSCGPGNLHLINGLFDCHRNHVPVLAIAAHIPSSEIGSGYFQETHPQELFRECSHYCELVSTPEQIPQVLAI 143
Cdd:PRK08978 61 TGKVGVCIATSGPGATNLITGLADALLDSVPVVAITGQVSSPLIGTDAFQEIDVLGLSLACTKHSFLVQSLEELPEIMAE 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 144 AMRKAVINRGVSVVV-LPGDVALKAAPesaSSHWYHAPLPQVTPAEEELKKLAQLLRYSSNIALMCGSGC--AGAHKELV 220
Cdd:PRK08978 141 AFEIASSGRPGPVLVdIPKDIQLAEGE---LEPHLTTVENEPAFPAAELEQARALLAQAKKPVLYVGGGVgmAGAVPALR 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 221 DFAAKLKAPIVHALRGKEHVEYDNPYDVGMTGLIGFSSGFHTMMNADTLVLLGTQFPYRA------FYPtDAKIIQIDIN 294
Cdd:PRK08978 218 EFLAATGMPAVATLKGLGAVEADHPYYLGMLGMHGTKAANLAVQECDLLIAVGARFDDRVtgklntFAP-HAKVIHLDID 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 295 PGSIGAHSKVDMALVGDIKSTLSALMPHLeektdrkfldkALEHYRDARKGLDDLAK-----PSDKtIHPQYLAQRISHY 369
Cdd:PRK08978 297 PAEINKLRQAHVALQGDLNALLPALQQPL-----------NIDAWRQHCAQLRAEHAwrydhPGEA-IYAPALLKQLSDR 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 370 ADDDAIFTCDVGTPTVWAARYLQMNGKRRLLGSFNHGSMANAMPQAIGAKATAPDRQVVAMCGDGGFSMLMGDFLSLAQM 449
Cdd:PRK08978 365 KPADTVVTTDVGQHQMWVAQHMRFTRPENFITSSGLGTMGFGLPAAIGAQVARPDDTVICVSGDGSFMMNVQELGTIKRK 444
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 450 KLPVKIVIFNNSVLGFVAMEMK---AGGY----LTDGtelhaTNFARIAEACGIKGIRVESASEVDEALQTAFATDGPVL 522
Cdd:PRK08978 445 QLPVKIVLLDNQRLGMVRQWQQlffDERYsetdLSDN-----PDFVMLASAFGIPGQTITRKDQVEAALDTLLNSEGPYL 519
|
....*....
gi 640683833 523 VDVVVASEE 531
Cdd:PRK08978 520 LHVSIDELE 528
|
|
| PRK07525 |
PRK07525 |
sulfoacetaldehyde acetyltransferase; Validated |
1-535 |
4.13e-60 |
|
sulfoacetaldehyde acetyltransferase; Validated
Pssm-ID: 236042 [Multi-domain] Cd Length: 588 Bit Score: 209.47 E-value: 4.13e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 1 MKQTVAAYIAKTLEQAGVKRIWGVTGDSLNGLSDSLNRMGtIDWMPTRHEEVAAFAAGAEAQLTGELAVCAGSCGPGNLH 80
Cdd:PRK07525 4 MKMTPSEAFVETLQAHGITHAFGIIGSAFMDASDLFPPAG-IRFIDVAHEQNAGHMADGYTRVTGRMGMVIGQNGPGITN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 81 LINGLFDCHRNHVPVLAIAAHIPSSEIGSGYFQETHPQELFRECSHYCELVSTPEQIPQVLAIAMRKAVINRGVSVVVLP 160
Cdd:PRK07525 83 FVTAVATAYWAHTPVVLVTPQAGTKTIGQGGFQEAEQMPMFEDMTKYQEEVRDPSRMAEVLNRVFDKAKRESGPAQINIP 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 161 GDvalkaapesassHWYH---APLPQV------TPAEEELKKLAQLLRYSSNIALMCGSGC--AGAHKELVDFAAKLKAP 229
Cdd:PRK07525 163 RD------------YFYGvidVEIPQPvrlergAGGEQSLAEAAELLSEAKFPVILSGAGVvlSDAIEECKALAERLDAP 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 230 IVHALRGKEHVEYDNPYDVGMTGLIGFSSGFHTMMNADTLVLLGTQF-PYRA-------FYPTDAKIIQIDINPGSIGAH 301
Cdd:PRK07525 231 VACGYLHNDAFPGSHPLWVGPLGYNGSKAAMELIAKADVVLALGTRLnPFGTlpqygidYWPKDAKIIQVDINPDRIGLT 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 302 SKVDMALVGDIKST-------LSALMPHLEEKTDRKFLDKA-----------LEHYRDArKGLDDLAKPSDKT---IHPQ 360
Cdd:PRK07525 311 KKVSVGICGDAKAVarellarLAERLAGDAGREERKALIAAeksaweqelssWDHEDDD-PGTDWNEEARARKpdyMHPR 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 361 YLAQRISHYADDDAIFTCDVGTPTVWAARYLQMNGKRRLLGSFNHGSMANAMPQAIGAKATAPDRQVVAMCGDGGFSMLM 440
Cdd:PRK07525 390 QALREIQKALPEDAIVSTDIGNNCSIANSYLRFEKGRKYLAPGSFGNCGYAFPAIIGAKIACPDRPVVGFAGDGAWGISM 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 441 GDFLSLAQMKLPVKIVIFNNSVLG-------------FVamemkaggyltdGTELHA-TNFARIAEACGIKGIRVESASE 506
Cdd:PRK07525 470 NEVMTAVRHNWPVTAVVFRNYQWGaekknqvdfynnrFV------------GTELDNnVSYAGIAEAMGAEGVVVDTQEE 537
|
570 580 590
....*....|....*....|....*....|.
gi 640683833 507 VDEALQTAFA--TDGPVLVDVVVASEELAMP 535
Cdd:PRK07525 538 LGPALKRAIDaqNEGKTTVIEIMCNQELGEP 568
|
|
| PRK06466 |
PRK06466 |
acetolactate synthase 3 large subunit; |
6-539 |
6.70e-60 |
|
acetolactate synthase 3 large subunit;
Pssm-ID: 180578 [Multi-domain] Cd Length: 574 Bit Score: 208.83 E-value: 6.70e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 6 AAYIAKTLEQAGVKRIWGVTGDSLNGLSDSLNRMGTIDWMPTRHEEVAAFAAGAEAQLTGELAVCAGSCGPGNLHLINGL 85
Cdd:PRK06466 7 AEMLVRALRDEGVEYIYGYPGGAVLHIYDALFKQDKVEHILVRHEQAATHMADGYARATGKTGVVLVTSGPGATNAITGI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 86 FDCHRNHVPVLAIAAHIPSSEIGSGYFQETHPQELFRECSHYCELVSTPEQIPQVLAIAMRKAVINRGVSVVV-LPGDVA 164
Cdd:PRK06466 87 ATAYMDSIPMVVLSGQVPSTLIGEDAFQETDMVGISRPIVKHSFMVKHASEIPEIIKKAFYIAQSGRPGPVVVdIPKDMT 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 165 LKAA------PESASSHWYHaplPQVTPAEEELKKLAQLLRYSSNIALMCGSGC--AGAHKELVDFAAKLKAPIVHALRG 236
Cdd:PRK06466 167 NPAEkfeyeyPKKVKLRSYS---PAVRGHSGQIRKAVEMLLAAKRPVIYSGGGVvlGNASALLTELAHLLNLPVTNTLMG 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 237 KEHVEYDNPYDVGMTGLIGFSSGFHTMMNADTLVLLGTQFPYRA------FYPtDAKIIQIDINPGSIGAHSKVDMALVG 310
Cdd:PRK06466 244 LGGFPGTDRQFLGMLGMHGTYEANMAMHHADVILAVGARFDDRVtngpakFCP-NAKIIHIDIDPASISKTIKADIPIVG 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 311 DIKSTLS---ALMPHLEEKTDRKFLD---KALEHYRdARKGLDDLAKPSDKTIHPQYLAQRISHYADDDAIFTCDVGTPT 384
Cdd:PRK06466 323 PVESVLTemlAILKEIGEKPDKEALAawwKQIDEWR-GRHGLFPYDKGDGGIIKPQQVVETLYEVTNGDAYVTSDVGQHQ 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 385 VWAARYLQMNGKRRLLGSFNHGSMANAMPQAIGAKATAPDRQVVAMCGDGGFSMLMGDFLSLAQMKLPVKIVIFNNSVLG 464
Cdd:PRK06466 402 MFAAQYYKFNKPNRWINSGGLGTMGFGLPAAMGVKLAFPDQDVACVTGEGSIQMNIQELSTCLQYGLPVKIINLNNGALG 481
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 640683833 465 FVA--MEMKAGGYLTDGTELHATNFARIAEACGIKGIRVESASEVDEALQTAFA-TDGPVLVDVVVASEELAMPPQIK 539
Cdd:PRK06466 482 MVRqwQDMQYEGRHSHSYMESLPDFVKLAEAYGHVGIRITDLKDLKPKLEEAFAmKDRLVFIDIYVDRSEHVYPMQIA 559
|
|
| PRK06882 |
PRK06882 |
acetolactate synthase 3 large subunit; |
2-539 |
5.85e-59 |
|
acetolactate synthase 3 large subunit;
Pssm-ID: 168717 [Multi-domain] Cd Length: 574 Bit Score: 206.30 E-value: 5.85e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 2 KQTVAAYIAKTLEQAGVKRIWGVTGDSLNGLSDSLNRMGTIDWMPTRHEEVAAFAAGAEAQLTGELAVCAGSCGPGNLHL 81
Cdd:PRK06882 3 KLSGAEMVVQSLRDEGVEYVFGYPGGSVLDIYDAIHTLGGIEHVLVRHEQAAVHMADGYARSTGKVGCVLVTSGPGATNA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 82 INGLFDCHRNHVPVLAIAAHIPSSEIGSGYFQETHPQELFRECSHYCELVSTPEQIPQVLAIAMRKAVINRGVSVVV-LP 160
Cdd:PRK06882 83 ITGIATAYTDSVPLVILSGQVPSNLIGTDAFQECDMLGISRPVVKHSFIVKNAEDIPSTIKKAFYIASTGRPGPVVIdIP 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 161 GDVALKAA------PESASSHWYHaplPQVTPAEEELKKLAQLLRYSSNIALMCGSGC--AGAHKELVDFAAKLKAPIVH 232
Cdd:PRK06882 163 KDMVNPANkftyeyPEEVSLRSYN---PTVQGHKGQIKKALKALLVAKKPVLFVGGGVitAECSEQLTQFAQKLNLPVTS 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 233 ALRGKEHVEYDNPYDVGMTGLIGFSSGFHTMMNADTLVLLGTQFPYR-----AFYPTDAKIIQIDINPGSIGAHSKVDMA 307
Cdd:PRK06882 240 SLMGLGAYPSTDKQFLGMLGMHGTYEANNAMHESDLILGIGVRFDDRttnnlAKYCPNAKVIHIDIDPTSISKNVPAYIP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 308 LVGDIKSTLSALMPHLEE------KTDRKFLDKALEHYRdARKGLDdlAKPSDKTIHPQYLAQRISHYADDDAIFTCDVG 381
Cdd:PRK06882 320 IVGSAKNVLEEFLSLLEEenlaksQTDLTAWWQQINEWK-AKKCLE--FDRTSDVIKPQQVVEAIYRLTNGDAYVASDVG 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 382 TPTVWAARYLQMNGKRRLLGSFNHGSMANAMPQAIGAKATAPDRQVVAMCGDGGFSMLMGDFLSLAQMKLPVKIVIFNNS 461
Cdd:PRK06882 397 QHQMFAALHYPFDKPRRWINSGGAGTMGFGLPAAIGVKFAHPEATVVCVTGDGSIQMNIQELSTAKQYDIPVVIVSLNNR 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 462 VLGFVA--MEMKAGGYLTDGTELHATNFARIAEACGIKGIRVESASEVDEALQTAFAT-DGPVLVDVVVASEELAMPPQI 538
Cdd:PRK06882 477 FLGMVKqwQDLIYSGRHSQVYMNSLPDFAKLAEAYGHVGIQIDTPDELEEKLTQAFSIkDKLVFVDVNVDETEHVYPMQI 556
|
.
gi 640683833 539 K 539
Cdd:PRK06882 557 R 557
|
|
| PRK06456 |
PRK06456 |
acetolactate synthase large subunit; |
6-542 |
1.05e-58 |
|
acetolactate synthase large subunit;
Pssm-ID: 180569 [Multi-domain] Cd Length: 572 Bit Score: 205.46 E-value: 1.05e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 6 AAYIAKTLEQAGVKRIWGVTGDSLNGLSDSLN---RMGTIDWMPTRHEEVAAFAAGAEAQLTGELAVCAGSCGPGNLHLI 82
Cdd:PRK06456 5 ARILVDSLKREGVKVIFGIPGLSNMQIYDAFVedlANGELRHVLMRHEQAAAHAADGYARASGVPGVCTATSGPGTTNLV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 83 NGLFDCHRNHVPVLAIAAHIPSSEIGSGYFQETHPQELFRECSHYCELVSTPEQIPQVLAIAMRKAVINR-GVSVVVLPG 161
Cdd:PRK06456 85 TGLITAYWDSSPVIAITGQVPRSVMGKMAFQEADAMGVFENVTKYVIGIKRIDEIPQWIKNAFYIATTGRpGPVVIDIPR 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 162 DVALKAA-----PESASSHWYHaPLPQVTPaEEELKKLAQLLRYSSNIALMCGSGC--AGAHKELVDFAAKLKAPIVHAL 234
Cdd:PRK06456 165 DIFYEKMeeikwPEKPLVKGYR-DFPTRID-RLALKKAAEILINAERPIILVGTGVvwSNATPEVLELAELLHIPIVSTF 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 235 RGKEHVEYDNPYDVGMTGLIGFSSGFHTMMNADTLVLLGTQFPYRAFYP------TDAKIIQIDINPGSIGAHSKVDMAL 308
Cdd:PRK06456 243 PGKTAIPHDHPLYFGPMGYYGRAEASMAALESDAMLVVGARFSDRTFTSydemveTRKKFIMVNIDPTDGEKAIKVDVGI 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 309 VGDIKSTLSALM---PHLEEKTDRKFLDKALEHYRDARKGLddLAKPSDKTIHPQYLAQRISHYADDDAIFTCDVGTPTV 385
Cdd:PRK06456 323 YGNAKIILRELIkaiTELGQKRDRSAWLKRVKEYKEYYSQF--YYTEENGKLKPWKIMKTIRQALPRDAIVTTGVGQHQM 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 386 WAARYLQMNGKRRLLGSFNHGSMANAMPQAIGAKATAPDRQVVAMCGDGGFSMLMGDFLSLAQMKLPVKIVIFNNSVLGF 465
Cdd:PRK06456 401 WAEVFWEVLEPRTFLTSSGMGTMGFGLPAAMGAKLARPDKVVVDLDGDGSFLMTGTNLATAVDEHIPVISVIFDNRTLGL 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 466 V--AMEMKAGGYLTDGTELHATNFARIAEACGIKGIRVESASEVDEALQTAFATDGPVLVDVVVASEELA---MPPQIKL 540
Cdd:PRK06456 481 VrqVQDLFFGKRIVGVDYGPSPDFVKLAEAFGALGFNVTTYEDIEKSLKSAIKEDIPAVIRVPVDKEELAlptLPPGGRL 560
|
..
gi 640683833 541 EQ 542
Cdd:PRK06456 561 KQ 562
|
|
| PRK06112 |
PRK06112 |
acetolactate synthase catalytic subunit; Validated |
4-536 |
2.93e-58 |
|
acetolactate synthase catalytic subunit; Validated
Pssm-ID: 235700 [Multi-domain] Cd Length: 578 Bit Score: 204.22 E-value: 2.93e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 4 TVAAYIAKTLEQAGVKRIWGVTGDSLNGLSDSLNRMGTIDWmptRHEEVAAFAAGAEAQLTGELAVCAGSCGPGNLHLIN 83
Cdd:PRK06112 15 TVAHAIARALKRHGVEQIFGQSLPSALFLAAEAIGIRQIAY---RTENAGGAMADGYARVSGKVAVVTAQNGPAATLLVA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 84 GLFDCHRNHVPVLAIAAHIPSSEIGSGYFQETHPQELFRECSHYCELVSTPEQIPQVLAIAMRKAVINR-GVSVVVLPGD 162
Cdd:PRK06112 92 PLAEALKASVPIVALVQDVNRDQTDRNAFQELDHIALFQSCTKWVRRVTVAERIDDYVDQAFTAATSGRpGPVVLLLPAD 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 163 VALKAAPESA---SSHWYHAPLPQVTPAEEELKKLAQLLRYSSNIALMCGSG--CAGAHKELVDFAAKLKAPIVHALRGK 237
Cdd:PRK06112 172 LLTAAAAAPAaprSNSLGHFPLDRTVPAPQRLAEAASLLAQAQRPVVVAGGGvhISGASAALAALQSLAGLPVATTNMGK 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 238 EHVEYDNPYDVGMTG-LIG-FSSGFHTM---MNADTLVLLGTQFPYRA-----FYPTDAKIIQIDINPGSIGAHSKVdMA 307
Cdd:PRK06112 252 GAVDETHPLSLGVVGsLMGpRSPGRHLRdlvREADVVLLVGTRTNQNGtdswsLYPEQAQYIHIDVDGEEVGRNYEA-LR 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 308 LVGDIKSTLSALMPHLE------EKTDRKFLDKALEHYRDA-RKGLDDLAKPSDKTIHPQYLAQRISHYADDDAIFTCDV 380
Cdd:PRK06112 331 LVGDARLTLAALTDALRgrdlaaRAGRRAALEPAIAAGREAhREDSAPVALSDASPIRPERIMAELQAVLTGDTIVVADA 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 381 GTPTVWAARYLQMNGKR-RLLGSFNHGSMANAMPQAIGAKATAPDRQVVAMCGDGGFSMLMGDFLSLAQMKLPVKIVIFN 459
Cdd:PRK06112 411 SYSSIWVANFLTARRAGmRFLTPRGLAGLGWGVPMAIGAKVARPGAPVICLVGDGGFAHVWAELETARRMGVPVTIVVLN 490
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 640683833 460 NSVLGFV--AMEMKAGGYlTDGTELHATNFARIAEACGIKGIRVESASEVDEALQTAFATDGPVLVDVVvaSEELAMPP 536
Cdd:PRK06112 491 NGILGFQkhAETVKFGTH-TDACHFAAVDHAAIARACGCDGVRVEDPAELAQALAAAMAAPGPTLIEVI--TDPSAFPP 566
|
|
| PRK07979 |
PRK07979 |
acetolactate synthase 3 large subunit; |
6-539 |
2.85e-57 |
|
acetolactate synthase 3 large subunit;
Pssm-ID: 181185 [Multi-domain] Cd Length: 574 Bit Score: 201.62 E-value: 2.85e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 6 AAYIAKTLEQAGVKRIWGVTGDSLNGLSDSLNRMGTIDWMPTRHEEVAAFAAGAEAQLTGELAVCAGSCGPGNLHLINGL 85
Cdd:PRK07979 7 AEMVVRSLIDQGVKQVFGYPGGAVLDIYDALHTVGGIDHVLVRHEQAAVHMADGLARATGEVGVVLVTSGPGATNAITGI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 86 FDCHRNHVPVLAIAAHIPSSEIGSGYFQETHPQELFRECSHYCELVSTPEQIPQVLAIAMRKAVINR-GVSVVVLPGDV- 163
Cdd:PRK07979 87 ATAYMDSIPLVVLSGQVATSLIGYDAFQECDMVGISRPVVKHSFLVKQTEDIPQVLKKAFWLAASGRpGPVVVDLPKDIl 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 164 --ALK---AAPESASSHWYHaplPQVTPAEEELKKLAQLLRYSSNIALMCGSGC--AGAHKELVDFAAKLKAPIVHALRG 236
Cdd:PRK07979 167 npANKlpyVWPESVSMRSYN---PTTQGHKGQIKRALQTLVAAKKPVVYVGGGAinAACHQQLKELVEKLNLPVVSSLMG 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 237 KEHVEYDNPYDVGMTGLIGFSSGFHTMMNADTLVLLGTQFPYR-----AFYPTDAKIIQIDINPGSIGAHSKVDMALVGD 311
Cdd:PRK07979 244 LGAFPATHRQSLGMLGMHGTYEANMTMHNADVIFAVGVRFDDRttnnlAKYCPNATVLHIDIDPTSISKTVTADIPIVGD 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 312 IKSTLSALMPHLEEKTDRKFLD------KALEHYRdARKGLDdlAKPSDKTIHPQYLAQRISHYADDDAIFTCDVGTPTV 385
Cdd:PRK07979 324 ARQVLEQMLELLSQESAHQPLDeirdwwQQIEQWR-ARQCLK--YDTHSEKIKPQAVIETLWRLTKGDAYVTSDVGQHQM 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 386 WAARYLQMNGKRRLLGSFNHGSMANAMPQAIGAKATAPDRQVVAMCGDGGFSMLMGDFLSLAQMKLPVKIVIFNNSVLGF 465
Cdd:PRK07979 401 FAALYYPFDKPRRWINSGGLGTMGFGLPAALGVKMALPEETVVCVTGDGSIQMNIQELSTALQYELPVLVLNLNNRYLGM 480
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 640683833 466 VA--MEMKAGGYLTDGTELHATNFARIAEACGIKGIRVESASEVDEALQTAFA---TDGPVLVDVVVASEELAMPPQIK 539
Cdd:PRK07979 481 VKqwQDMIYSGRHSQSYMQSLPDFVRLAEAYGHVGIQISHPDELESKLSEALEqvrNNRLVFVDVTVDGSEHVYPMQIR 559
|
|
| PRK08266 |
PRK08266 |
hypothetical protein; Provisional |
1-535 |
4.63e-57 |
|
hypothetical protein; Provisional
Pssm-ID: 181337 [Multi-domain] Cd Length: 542 Bit Score: 200.24 E-value: 4.63e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 1 MKQTVAAYIAKTLEQAGVKRIWGVTGDSLNGLSDSLNRMGT-IDWMPTRHEEVAAFAAGAEAQLTGELAVCAGSCGPGNL 79
Cdd:PRK08266 2 TTMTGGEAIVAGLVAHGVDTVFGLPGAQLYWLFDALYKAGDrIRVIHTRHEQAAGYMAFGYARSTGRPGVCSVVPGPGVL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 80 HLINGLFDCHRNHVPVLAIAAHIPSSEIGSGYFQ--ETHPQ-ELFRECSHYCELVSTPEQIPQVLAIAMRKAVINRGVSV 156
Cdd:PRK08266 82 NAGAALLTAYGCNSPVLCLTGQIPSALIGKGRGHlhEMPDQlATLRSFTKWAERIEHPSEAPALVAEAFQQMLSGRPRPV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 157 VV-LPGDVALKAAPESASSHWyhAPLPQVTPAEEELKKLAQLLRYSSNIALMCGSGCAGAHKELVDFAAKLKAPIVHALR 235
Cdd:PRK08266 162 ALeMPWDVFGQRAPVAAAPPL--RPAPPPAPDPDAIAAAAALIAAAKNPMIFVGGGAAGAGEEIRELAEMLQAPVVAFRS 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 236 GKEHVeyDNPYDVGMTgligFSSGFHTMMNADTLVLLGT----QFPYRAFYPTDAKIIQIDINPGSIGAHsKVDMALVGD 311
Cdd:PRK08266 240 GRGIV--SDRHPLGLN----FAAAYELWPQTDVVIGIGSrlelPTFRWPWRPDGLKVIRIDIDPTEMRRL-KPDVAIVAD 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 312 IKSTLSALMPHLEEKTDRKfldkalEHYRDARKGLDDLAKPSDKTIHPQ--YLaQRISHYADDDAIFT---CDVGtptvW 386
Cdd:PRK08266 313 AKAGTAALLDALSKAGSKR------PSRRAELRELKAAARQRIQAVQPQasYL-RAIREALPDDGIFVdelSQVG----F 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 387 AARY-LQMNGKRRLLGSFNHGSMANAMPQAIGAKATAPDRQVVAMCGDGGFSMLMGDFLSLAQMKLPVKIVIFNNSVLGF 465
Cdd:PRK08266 382 ASWFaFPVYAPRTFVTCGYQGTLGYGFPTALGAKVANPDRPVVSITGDGGFMFGVQELATAVQHNIGVVTVVFNNNAYGN 461
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 640683833 466 VAMEMK---AGGYLtdGTELHATNFARIAEACGIKGIRVESASEVDEALQTAFATDGPVLVDVVVASEELAMP 535
Cdd:PRK08266 462 VRRDQKrrfGGRVV--ASDLVNPDFVKLAESFGVAAFRVDSPEELRAALEAALAHGGPVLIEVPVPRGSEASP 532
|
|
| PRK09107 |
PRK09107 |
acetolactate synthase 3 catalytic subunit; Validated |
4-535 |
8.20e-57 |
|
acetolactate synthase 3 catalytic subunit; Validated
Pssm-ID: 236380 [Multi-domain] Cd Length: 595 Bit Score: 200.70 E-value: 8.20e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 4 TVAAYIAKTLEQAGVKRIWGVTGDSLNGLSDSLNRMGTIDWMPTRHEEVAAFAAGAEAQLTGELAVCAGSCGPGNLHLIN 83
Cdd:PRK09107 12 TGAEMVVQALKDQGVEHIFGYPGGAVLPIYDEIFQQDDIQHILVRHEQGAGHAAEGYARSTGKPGVVLVTSGPGATNAVT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 84 GLFDCHRNHVPVLAIAAHIPSSEIGSGYFQETHPQELFRECSHYCELVSTPEQIPQVLAIAMRKAVINRGVSVVV-LPGD 162
Cdd:PRK09107 92 PLQDALMDSIPLVCITGQVPTHLIGSDAFQECDTVGITRPCTKHNWLVKDVNDLARVIHEAFHVATSGRPGPVVVdIPKD 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 163 VALKA----APESASSHWYHAPLPQVTPaeEELKKLAQLLRYSSNIALMCGSGC----AGAHKELVDFAAKLKAPIVHAL 234
Cdd:PRK09107 172 VQFATgtytPPQKAPVHVSYQPKVKGDA--EAITEAVELLANAKRPVIYSGGGVinsgPEASRLLRELVELTGFPITSTL 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 235 RGKEHVEYDNPYDVGMTGLIGFSSGFHTMMNADTLVLLGTQFPYR------AFYPTdAKIIQIDINPGSIGAHSKVDMAL 308
Cdd:PRK09107 250 MGLGAYPASGKNWLGMLGMHGTYEANMAMHDCDVMLCVGARFDDRitgrldAFSPN-SKKIHIDIDPSSINKNVRVDVPI 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 309 VGDIKSTLSALMPHLE---EKTDRKFLDK---ALEHYRdARKGLDdlAKPSDKTIHPQYLAQRIshYA---DDDAIFTCD 379
Cdd:PRK09107 329 IGDVGHVLEDMLRLWKargKKPDKEALADwwgQIARWR-ARNSLA--YTPSDDVIMPQYAIQRL--YEltkGRDTYITTE 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 380 VGTPTVWAARYLQMNGKRRLLGSFNHGSMANAMPQAIGAKATAPDRQVVAMCGDGGFSMLMGDFLSLAQMKLPVKIVIFN 459
Cdd:PRK09107 404 VGQHQMWAAQFFGFEEPNRWMTSGGLGTMGYGLPAALGVQIAHPDALVIDIAGDASIQMCIQEMSTAVQYNLPVKIFILN 483
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 640683833 460 NSVLGFVA--MEMKAGGYLTDGTELHATNFARIAEACGIKGIRVESASEVDEALQTAFATDGPVLVDVVVASEELAMP 535
Cdd:PRK09107 484 NQYMGMVRqwQQLLHGNRLSHSYTEAMPDFVKLAEAYGAVGIRCEKPGDLDDAIQEMIDVDKPVIFDCRVANLENCFP 561
|
|
| acolac_catab |
TIGR02418 |
acetolactate synthase, catabolic; Acetolactate synthase (EC 2.2.1.6) combines two molecules of ... |
6-527 |
2.83e-56 |
|
acetolactate synthase, catabolic; Acetolactate synthase (EC 2.2.1.6) combines two molecules of pyruvate to yield 2-acetolactate with the release of CO2. This reaction may be involved in either valine biosynthesis (biosynthetic) or conversion of pyruvate to acetoin and possibly to 2,3-butanediol (catabolic). The biosynthetic type, described by TIGR00118, is also capable of forming acetohydroxybutyrate from pyruvate and 2-oxobutyrate for isoleucine biosynthesis. The family described here, part of the same larger family of thiamine pyrophosphate-dependent enzymes (pfam00205, pfam02776) is the catabolic form, generally found associated with in species with acetolactate decarboxylase and usually found in the same operon. The model may not encompass all catabolic acetolactate synthases, but rather one particular clade in the larger TPP-dependent enzyme family. [Energy metabolism, Fermentation]
Pssm-ID: 131471 [Multi-domain] Cd Length: 539 Bit Score: 198.05 E-value: 2.83e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 6 AAYIAKTLEQAGVKRIWGVTGDSLNGLSDSLNRMGtIDWMPTRHEEVAAFAAGAEAQLTGELAVCAGSCGPGNLHLINGL 85
Cdd:TIGR02418 2 ADLVVDQLENQGVRYVFGIPGAKIDRVFDALEDKG-IELIVVRHEQNAAFMAQAVGRITGKPGVALVTSGPGCSNLVTGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 86 FDCHRNHVPVLAIAAHIPSSEIGSGYFQETHPQELFRECSHYCELVSTPEQIPQVLAIAMRKAVINR-GVSVVVLPGDVA 164
Cdd:TIGR02418 81 ATANSEGDPVVAIGGQVKRADLLKLTHQSMDNVALFRPITKYSAEVQDPDALSEVVANAFRAAESGKpGAAFVSLPQDVV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 165 lkAAPESASShWYHAPLPQVTPA-EEELKKLAQLLRYSSNIALMCG--SGCAGAHKELVDFAAKLKAPIVHALRGKEHVE 241
Cdd:TIGR02418 161 --DSPVSVKA-IPASYAPKLGAApDDAIDEVAEAIQNAKLPVLLLGlrASSPETTEAVRRLLKKTQLPVVETFQGAGAVS 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 242 YDN-PYDVGMTGLIGFSSGFHTMMNADTLVLLG-TQFPYRAFY---PTDAKIIQIDINPGSIGAHSKVDMALVGDIKSTL 316
Cdd:TIGR02418 238 RELeDHFFGRVGLFRNQPGDRLLKQADLVITIGyDPIEYEPRNwnsENDATIVHIDVEPAQIDNNYQPDLELVGDIASTL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 317 SALMPHLEE----KTDRKFLdKALEHYRDARKGLDdlAKPSDKTIHPQYLAQRISHYADDDAIFTCDVGTPTVWAARYLQ 392
Cdd:TIGR02418 318 DLLAERIPGyelpPDALAIL-EDLKQQREALDRVP--ATLKQAHLHPLEIIKAMQAIVTDDVTVTVDMGSHYIWMARYFR 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 393 MNGKRRLLGSFNHGSMANAMPQAIGAKATAPDRQVVAMCGDGGFSMLMGDFLSLAQMKLPVKIVIFNNSVLGFVAM--EM 470
Cdd:TIGR02418 395 SYRARHLLISNGMQTLGVALPWAIGAALVRPNTKVVSVSGDGGFLFSSMELETAVRLKLNIVHIIWNDNGYNMVEFqeEM 474
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 640683833 471 KAGgyLTDGTELHATNFARIAEACGIKGIRVESASEVDEALQTAFATDGPVLVDVVV 527
Cdd:TIGR02418 475 KYQ--RSSGVDFGPIDFVKYAESFGAKGLRVESPDQLEPTLRQAMEVEGPVVVDIPV 529
|
|
| TPP_AHAS |
cd02015 |
Thiamine pyrophosphate (TPP) family, Acetohydroxyacid synthase (AHAS) subfamily, TPP-binding ... |
357-535 |
3.78e-55 |
|
Thiamine pyrophosphate (TPP) family, Acetohydroxyacid synthase (AHAS) subfamily, TPP-binding module; composed of proteins similar to the large catalytic subunit of AHAS. AHAS catalyzes the condensation of two molecules of pyruvate to give the acetohydroxyacid, 2-acetolactate. 2-Acetolactate is the precursor of the branched chain amino acids, valine and leucine. AHAS also catalyzes the condensation of pyruvate and 2-ketobutyrate to form 2-aceto-2-hydroxybutyrate in isoleucine biosynthesis. In addition to requiring TPP and a divalent metal ion as cofactors, AHAS requires FAD.
Pssm-ID: 238973 [Multi-domain] Cd Length: 186 Bit Score: 184.24 E-value: 3.78e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 357 IHPQYLAQRISHYADDDAIFTCDVGTPTVWAARYLQMNGKRRLLGSFNHGSMANAMPQAIGAKATAPDRQVVAMCGDGGF 436
Cdd:cd02015 1 IKPQEVIKELSELTPGDAIVTTDVGQHQMWAAQYYRFKKPRSWLTSGGLGTMGFGLPAAIGAKVARPDKTVICIDGDGSF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 437 SMLMGDFLSLAQMKLPVKIVIFNNSVLGFVA--MEMKAGGYLTDGTELHATNFARIAEACGIKGIRVESASEVDEALQTA 514
Cdd:cd02015 81 QMNIQELATAAQYNLPVKIVILNNGSLGMVRqwQELFYEGRYSHTTLDSNPDFVKLAEAYGIKGLRVEKPEELEAALKEA 160
|
170 180
....*....|....*....|.
gi 640683833 515 FATDGPVLVDVVVASEELAMP 535
Cdd:cd02015 161 LASDGPVLLDVLVDPEENVLP 181
|
|
| PRK08617 |
PRK08617 |
acetolactate synthase AlsS; |
1-527 |
5.40e-54 |
|
acetolactate synthase AlsS;
Pssm-ID: 236312 [Multi-domain] Cd Length: 552 Bit Score: 191.99 E-value: 5.40e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 1 MKQTVAAYIAKTLEQAGVKRIWGVTG---DSL-NGLSDSlnrmgTIDWMPTRHEEVAAFAAGAEAQLTGELAVCAGSCGP 76
Cdd:PRK08617 3 KKKYGADLVVDSLINQGVKYVFGIPGakiDRVfDALEDS-----GPELIVTRHEQNAAFMAAAIGRLTGKPGVVLVTSGP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 77 GNLHLINGLFDCHRNHVPVLAIAAHIPSSEIGSGYFQETHPQELFRECSHYCELVSTPEQIPQVLAIAMRKAVINR-GVS 155
Cdd:PRK08617 78 GVSNLATGLVTATAEGDPVVAIGGQVKRADRLKRTHQSMDNVALFRPITKYSAEVQDPDNLSEVLANAFRAAESGRpGAA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 156 VVVLPGDVALKAAPESASSHwyhAPLPQVTPA-EEELKKLAQLLRYSSNIALMCG--SGCAGAHKELVDFAAKLKAPIVH 232
Cdd:PRK08617 158 FVSLPQDVVDAPVTSKAIAP---LSKPKLGPAsPEDINYLAELIKNAKLPVLLLGmrASSPEVTAAIRRLLERTNLPVVE 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 233 ALRGKEHV--EYDNPYdVGMTGLIGFSSGFHTMMNADTLVLLGtqfpYRAF-Y-------PTDAKIIQIDINPGSIGAHS 302
Cdd:PRK08617 235 TFQAAGVIsrELEDHF-FGRVGLFRNQPGDELLKKADLVITIG----YDPIeYeprnwnsEGDATIIHIDVLPAEIDNYY 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 303 KVDMALVGDIKSTLSALMPHLEEktdRKFLDKALEHYRDARKGLDDLAKP----SDKTIHPQYLAQRISHYADDDAIFTC 378
Cdd:PRK08617 310 QPERELIGDIAATLDLLAEKLDG---LSLSPQSLEILEELRAQLEELAERparlEEGAVHPLRIIRALQDIVTDDTTVTV 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 379 DVGTPTVWAARYLQMNGKRRLLGSFNHGSMANAMPQAIGAKATAPDRQVVAMCGDGGFsMLMGDFLSLA-QMKLPVKIVI 457
Cdd:PRK08617 387 DVGSHYIWMARYFRSYEPRHLLFSNGMQTLGVALPWAIAAALVRPGKKVVSVSGDGGF-LFSAMELETAvRLKLNIVHII 465
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 640683833 458 FNNSVLGFVAM--EMKAGGylTDGTELHATNFARIAEACGIKGIRVESASEVDEALQTAFATDGPVLVDVVV 527
Cdd:PRK08617 466 WNDGHYNMVEFqeEMKYGR--SSGVDFGPVDFVKYAESFGAKGLRVTSPDELEPVLREALATDGPVVIDIPV 535
|
|
| TPP_enzyme_C |
pfam02775 |
Thiamine pyrophosphate enzyme, C-terminal TPP binding domain; |
379-525 |
6.34e-53 |
|
Thiamine pyrophosphate enzyme, C-terminal TPP binding domain;
Pssm-ID: 460689 [Multi-domain] Cd Length: 151 Bit Score: 177.39 E-value: 6.34e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 379 DVGTPTVWAARYLQMNGKRRLLGSFNHGSMANAMPQAIGAKATAPDRQVVAMCGDGGFSMLMGDFLSLAQMKLPVKIVIF 458
Cdd:pfam02775 1 DIGCHQMWAAQYYRFRPPRRYLTSGGLGTMGYGLPAAIGAKLARPDRPVVAIAGDGGFQMNLQELATAVRYNLPITVVVL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 640683833 459 NNSVLGFVAMEMKAGG----YLTDGTELHATNFARIAEACGIKGIRVESASEVDEALQTAFATDGPVLVDV 525
Cdd:pfam02775 81 NNGGYGMTRGQQTPFGggrySGPSGKILPPVDFAKLAEAYGAKGARVESPEELEEALKEALEHDGPALIDV 151
|
|
| PRK08322 |
PRK08322 |
acetolactate synthase large subunit; |
11-527 |
7.02e-51 |
|
acetolactate synthase large subunit;
Pssm-ID: 236239 [Multi-domain] Cd Length: 547 Bit Score: 183.49 E-value: 7.02e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 11 KTLEQAGVKRIWGVTG----DSLNGLSDSlnrmgTIDWMPTRHEEVAAFAAGAEAQLTGELAVCAGSCGPGNLHLINGLF 86
Cdd:PRK08322 9 KCLENEGVEYIFGIPGeenlDLLEALRDS-----SIKLILTRHEQGAAFMAATYGRLTGKAGVCLSTLGPGATNLVTGVA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 87 DCHRNHVPVLAIAAHIP--SSEIGSgyFQETHPQELFRECSHYCELVSTPEQIPQVLAIAMRKAVINR-GVSVVVLPGDV 163
Cdd:PRK08322 84 YAQLGGMPMVAITGQKPikRSKQGS--FQIVDVVAMMAPLTKWTRQIVSPDNIPEVVREAFRLAEEERpGAVHLELPEDI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 164 AlkaaPESASSHwyhaPLPQ-----VTPAEEELKKLAQLLRYSSNIALMCGSGC--AGAHKELVDFAAKLKAPIVHALRG 236
Cdd:PRK08322 162 A----AEETDGK----PLPRsysrrPYASPKAIERAAEAIQAAKNPLILIGAGAnrKTASKALTEFVDKTGIPFFTTQMG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 237 KEHVEYDNPYDVGMTGL-----IGFssGFHtmmNADTLVLLGTQF----PYRAFYPTDAKIIQIDINPGSIGAHSKVDMA 307
Cdd:PRK08322 234 KGVIPETHPLSLGTAGLsqgdyVHC--AIE---HADLIINVGHDViekpPFFMNPNGDKKVIHINFLPAEVDPVYFPQVE 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 308 LVGDIKSTLSALMPHLEEKTDRKFldKALEHYRDA-RKGLDDLAKPSDKTIHPQYLAQRISHYADDDAIFTCDVGTPTVW 386
Cdd:PRK08322 309 VVGDIANSLWQLKERLADQPHWDF--PRFLKIREAiEAHLEEGADDDRFPMKPQRIVADLRKVMPDDDIVILDNGAYKIW 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 387 AARYLQMNGKRRLLGSFNHGSMANAMPQAIGAKATAPDRQVVAMCGDGGFSMLMGDFLSLAQMKLPVKIVIFNNSVLGFV 466
Cdd:PRK08322 387 FARNYRAYEPNTCLLDNALATMGAGLPSAIAAKLVHPDRKVLAVCGDGGFMMNSQELETAVRLGLPLVVLILNDNAYGMI 466
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 640683833 467 AMEMKAGGYLTDGTELHATNFARIAEACGIKGIRVESASEVDEALQTAFATDGPVLVDVVV 527
Cdd:PRK08322 467 RWKQENMGFEDFGLDFGNPDFVKYAESYGAKGYRVESADDLLPTLEEALAQPGVHVIDCPV 527
|
|
| TPP_enzymes |
cd00568 |
Thiamine pyrophosphate (TPP) enzyme family, TPP-binding module; found in many key metabolic ... |
362-527 |
1.13e-46 |
|
Thiamine pyrophosphate (TPP) enzyme family, TPP-binding module; found in many key metabolic enzymes which use TPP (also known as thiamine diphosphate) as a cofactor. These enzymes include, among others, the E1 components of the pyruvate, the acetoin and the branched chain alpha-keto acid dehydrogenase complexes.
Pssm-ID: 238318 [Multi-domain] Cd Length: 168 Bit Score: 161.27 E-value: 1.13e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 362 LAQRISHYADDDAIFTCDVGTPTVWAARYLQMNGKRRLLGSFNHGSMANAMPQAIGAKATAPDRQVVAMCGDGGFSMLMG 441
Cdd:cd00568 2 VLAALRAALPEDAIVVNDAGNSAYWAYRYLPLRRGRRFLTSTGFGAMGYGLPAAIGAALAAPDRPVVCIAGDGGFMMTGQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 442 DFLSLAQMKLPVKIVIFNNSVLGFVAMEMKAGGYLTD-GTELHATNFARIAEACGIKGIRVESASEVDEALQTAFATDGP 520
Cdd:cd00568 82 ELATAVRYGLPVIVVVFNNGGYGTIRMHQEAFYGGRVsGTDLSNPDFAALAEAYGAKGVRVEDPEDLEAALAEALAAGGP 161
|
....*..
gi 640683833 521 VLVDVVV 527
Cdd:cd00568 162 ALIEVKT 168
|
|
| PRK07064 |
PRK07064 |
thiamine pyrophosphate-binding protein; |
1-539 |
4.97e-45 |
|
thiamine pyrophosphate-binding protein;
Pssm-ID: 180820 [Multi-domain] Cd Length: 544 Bit Score: 167.09 E-value: 4.97e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 1 MKQTVAAYIAKTLEQAGVKRIWGVTgdSLNGLS--DSLNRMGTIDWMPTRHEEVAAFAAGAEAQLTGELAVCAGSCGPGN 78
Cdd:PRK07064 1 EKVTVGELIAAFLEQCGVKTAFGVI--SIHNMPilDAIGRRGKIRFVPARGEAGAVNMADAHARVSGGLGVALTSTGTGA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 79 LHLINGLFDCHRNHVPVLAIAAHIPSSEIGS--GYFQETHPQ-ELFRECSHYCELVSTPEQIPQVLAIAMRKAVINRGVS 155
Cdd:PRK07064 79 GNAAGALVEALTAGTPLLHITGQIETPYLDQdlGYIHEAPDQlTMLRAVSKAAFRVRSAETALATIREAVRVALTAPTGP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 156 VVV-LPGDV--ALKAAPESASShwyhAPLPQVTPAEEELKKLAQLLRYSSNIALMCGSGCAGAHKELVDFAAkLKAPIVH 232
Cdd:PRK07064 159 VSVeIPIDIqaAEIELPDDLAP----VHVAVPEPDAAAVAELAERLAAARRPLLWLGGGARHAGAEVKRLVD-LGFGVVT 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 233 ALRGKEHVEYDNPYDVGMTGLIGFSSGFHTmmNADTLVLLGTQF------PYRAFYPTDakIIQIDINPGSIGAHSKVDM 306
Cdd:PRK07064 234 STQGRGVVPEDHPASLGAFNNSAAVEALYK--TCDLLLVVGSRLrgnetlKYSLALPRP--LIRVDADAAADGRGYPNDL 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 307 ALVGDIKSTLSALMPHLEE--KTDRKFlDKALEHYRDA-----RKGLDDLAKpsdktihpqyLAQRISHYADDDAIFTCD 379
Cdd:PRK07064 310 FVHGDAARVLARLADRLEGrlSVDPAF-AADLRAAREAavadlRKGLGPYAK----------LVDALRAALPRDGNWVRD 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 380 VGTP-TVWAARYLQMNGKRRLLGSFNhGSMANAMPQAIGAKATAPDRQVVAMCGDGGFSMLMGDFLSLAQMKLPVKIVIF 458
Cdd:PRK07064 379 VTISnSTWGNRLLPIFEPRANVHALG-GGIGQGLAMAIGAALAGPGRKTVGLVGDGGLMLNLGELATAVQENANMVIVLM 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 459 NNSVLGFV-AMEMKAGGYLTDGTELHATNFARIAEACGIKGIRVESASEVDEALQTAFATDGPVLVDVVVAS-----EEL 532
Cdd:PRK07064 458 NDGGYGVIrNIQDAQYGGRRYYVELHTPDFALLAASLGLPHWRVTSADDFEAVLREALAKEGPVLVEVDMLSigpfaAAF 537
|
....*..
gi 640683833 533 AMPPQIK 539
Cdd:PRK07064 538 AGPPVKK 544
|
|
| PRK08199 |
PRK08199 |
thiamine pyrophosphate protein; Validated |
1-542 |
5.27e-41 |
|
thiamine pyrophosphate protein; Validated
Pssm-ID: 181285 [Multi-domain] Cd Length: 557 Bit Score: 156.19 E-value: 5.27e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 1 MKQTVAAYIAKTLEQAGVKRIWGVTGDSLNGLSDSLNRMGTIDWMPTRHEEVAAFAAGAEAQLTGELAVCAGSCGPGNLH 80
Cdd:PRK08199 6 RARTGGQILVDALRANGVERVFCVPGESYLAVLDALHDETDIRVIVCRQEGGAAMMAEAYGKLTGRPGICFVTRGPGATN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 81 LINGLFDCHRNHVPVLAIAAHIPSSEIGSGYFQETHPQELFRECSHYCELVSTPEQIPQVLAIAMRKAVINR-GVSVVVL 159
Cdd:PRK08199 86 ASIGVHTAFQDSTPMILFVGQVARDFREREAFQEIDYRRMFGPMAKWVAEIDDAARIPELVSRAFHVATSGRpGPVVLAL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 160 PGDVaLKAAPESASSHWYHAPLPQvtPAEEELKKLAQLL-RYSSNIALMCGSG-CAGAHKELVDFAAKLKAPIVHALRGK 237
Cdd:PRK08199 166 PEDV-LSETAEVPDAPPYRRVAAA--PGAADLARLAELLaRAERPLVILGGSGwTEAAVADLRAFAERWGLPVACAFRRQ 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 238 EHVEYDNPYDVGMTGLiGFSSGF-HTMMNADTLVLLGTQFP------YRAF---YPtDAKIIQIDINPGSIGAHSKVDMA 307
Cdd:PRK08199 243 DLFDNRHPNYAGDLGL-GINPALaARIREADLVLAVGTRLGevttqgYTLLdipVP-RQTLVHVHPDAEELGRVYRPDLA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 308 LVGDIKSTLSALM----PHLEEKTDRkfLDKALEHYRDARKglddlAKPSDKTIHPQYLAQRISHYADDDAIFTCDVGTP 383
Cdd:PRK08199 321 IVADPAAFAAALAalepPASPAWAEW--TAAAHADYLAWSA-----PLPGPGAVQLGEVMAWLRERLPADAIITNGAGNY 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 384 TVWAARYLQMNGKRRLLGSFNhGSMANAMPQAIGAKATAPDRQVVAMCGDGGFSMLMGDFLSLAQMKLPVKIVIFNNSVL 463
Cdd:PRK08199 394 ATWLHRFFRFRRYRTQLAPTS-GSMGYGLPAAIAAKLLFPERTVVAFAGDGCFLMNGQELATAVQYGLPIIVIVVNNGMY 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 464 GFVAM--EMKAGGYlTDGTELHATNFARIAEACGIKGIRVESASEVDEALQTAFATDGPVLVDVVVASEELAmpPQIKLE 541
Cdd:PRK08199 473 GTIRMhqEREYPGR-VSGTDLTNPDFAALARAYGGHGETVERTEDFAPAFERALASGKPALIEIRIDPEAIT--PTATLS 549
|
.
gi 640683833 542 Q 542
Cdd:PRK08199 550 Q 550
|
|
| PRK08327 |
PRK08327 |
thiamine pyrophosphate-requiring protein; |
62-528 |
2.96e-39 |
|
thiamine pyrophosphate-requiring protein;
Pssm-ID: 236243 [Multi-domain] Cd Length: 569 Bit Score: 151.31 E-value: 2.96e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 62 QLTGELAVCAGSCGPGNLHLINGLFDCHRNHVPVLAIAAHIPSSEIGS--------GYFQETHPQ-ELFRECSHYCELVS 132
Cdd:PRK08327 71 LVTGKPQAVMVHVDVGTANALGGVHNAARSRIPVLVFAGRSPYTEEGElgsrntriHWTQEMRDQgGLVREYVKWDYEIR 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 133 TPEQIPQVLAIAMRKAVIN-RGVSVVVLPGDVALKAAPESASSHWYHAPLPQVTPAEEELKKLAQLLRYSSNIALMC--G 209
Cdd:PRK08327 151 RGDQIGEVVARAIQIAMSEpKGPVYLTLPREVLAEEVPEVKADAGRQMAPAPPAPDPEDIARAAEMLAAAERPVIITwrA 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 210 SGCAGAHKELVDFAAKLKAPIVHAlRGkEHVEYdnPYDVGMtgLIGFSSGFhTMMNADTLVLLGTQFPY---RAFYPTDA 286
Cdd:PRK08327 231 GRTAEGFASLRRLAEELAIPVVEY-AG-EVVNY--PSDHPL--HLGPDPRA-DLAEADLVLVVDSDVPWipkKIRPDADA 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 287 KIIQIDINPgsigAHSK-------VDMALVGDIKSTLSALMPHL--EEKTDRKFLDKALEHYRDARKgLDDLAK------ 351
Cdd:PRK08327 304 RVIQIDVDP----LKSRiplwgfpCDLCIQADTSTALDQLEERLksLASAERRRARRRRAAVRELRI-RQEAAKraeier 378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 352 -PSDKTIHPQYLAQRISHYADD-DAIFTcdvGTPTVWaaRYLQMNGKRRLLGSFNHGSMANAMPQAIGAKATAPDRQVVA 429
Cdd:PRK08327 379 lKDRGPITPAYLSYCLGEVADEyDAIVT---EYPFVP--RQARLNKPGSYFGDGSAGGLGWALGAALGAKLATPDRLVIA 453
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 430 MCGDGGFsmLMGD---FLSLAQ-MKLPVKIVIFNNSVLGFVA---MEMKAGGY--------LTDGTElhATNFARIAEAC 494
Cdd:PRK08327 454 TVGDGSF--IFGVpeaAHWVAErYGLPVLVVVFNNGGWLAVKeavLEVYPEGYaarkgtfpGTDFDP--RPDFAKIAEAF 529
|
490 500 510
....*....|....*....|....*....|....*...
gi 640683833 495 GIKGIRVESASEVDEALQTAFA--TDG--PVLVDVVVA 528
Cdd:PRK08327 530 GGYGERVEDPEELKGALRRALAavRKGrrSAVLDVIVD 567
|
|
| PRK06154 |
PRK06154 |
thiamine pyrophosphate-requiring protein; |
5-535 |
3.33e-39 |
|
thiamine pyrophosphate-requiring protein;
Pssm-ID: 235718 [Multi-domain] Cd Length: 565 Bit Score: 151.12 E-value: 3.33e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 5 VAAYIAKTLEQAGVKRIWGVtgdSLNGLSDSLNRMGtIDWMPTRHEEVAAFAAGAEAQLTG--ELAVCAGSCGPGNLHLI 82
Cdd:PRK06154 22 VAEAVAEILKEEGVELLFGF---PVNELFDAAAAAG-IRPVIARTERVAVHMADGYARATSgeRVGVFAVQYGPGAENAF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 83 NGLFDCHRNHVPVLAIAAHIPSSEigsgyfQETHPQ----ELFRECSHYCELVSTPEQIPQVLAIAMRKAVINRGVSVVV 158
Cdd:PRK06154 98 GGVAQAYGDSVPVLFLPTGYPRGS------TDVAPNfeslRNYRHITKWCEQVTLPDEVPELMRRAFTRLRNGRPGPVVL 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 159 -LPGDVALKAAPESASSHwyhAPLPQVTPAEE--ELKKLAQLLRYSSNIALMCGSGC--AGAHKELVDFAAKLKAPIVHA 233
Cdd:PRK06154 172 eLPVDVLAEELDELPLDH---RPSRRSRPGADpvEVVEAAALLLAAERPVIYAGQGVlyAQATPELKELAELLEIPVMTT 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 234 LRGKEHVEYDNPYDVGMTGLIGFSSGFHTMMNADTLVLLGTQFPYRAF---YPTDAKIIQIDINPGSIGAHSKVDMALVG 310
Cdd:PRK06154 249 LNGKSAFPEDHPLALGSGGRARPATVAHFLREADVLFGIGCSLTRSYYglpMPEGKTIIHSTLDDADLNKDYPIDHGLVG 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 311 DIKSTLSALMPHLEEKTDRKFLDKA-----LEHYRDA--RKGLDDLAKpSDKTIHPQYLAQRISH-YADDDAIFTCDVGT 382
Cdd:PRK06154 329 DAALVLKQMIEELRRRVGPDRGRAQqvaaeIEAVRAAwlAKWMPKLTS-DSTPINPYRVVWELQHaVDIKTVIITHDAGS 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 383 P-----TVWAAR----YLQMnGKRRLLGSfnhgsmanAMPQAIGAKATAPDRQVVAMCGDGGFSMLMGDFLSLAQMKLPV 453
Cdd:PRK06154 408 PrdqlsPFYVASrpgsYLGW-GKTTQLGY--------GLGLAMGAKLARPDALVINLWGDAAFGMTGMDFETAVRERIPI 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 454 KIVIFNNSVLGFVAMEMKAggyltdGTELHATNF-----ARIAEACGIKGIRVESASEVDEALQTAF--ATDG-PVLVDV 525
Cdd:PRK06154 479 LTILLNNFSMGGYDKVMPV------STTKYRATDisgdyAAIARALGGYGERVEDPEMLVPALLRALrkVKEGtPALLEV 552
|
570
....*....|.
gi 640683833 526 VVASE-ELAMP 535
Cdd:PRK06154 553 ITSEEtALSRP 563
|
|
| PRK07524 |
PRK07524 |
5-guanidino-2-oxopentanoate decarboxylase; |
64-528 |
1.41e-38 |
|
5-guanidino-2-oxopentanoate decarboxylase;
Pssm-ID: 236041 [Multi-domain] Cd Length: 535 Bit Score: 148.97 E-value: 1.41e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 64 TGELAVCAGSCGPGNLHLINGLFDCHRNHVPVLAIAA--HIPSSEIGSGYFQETHPQE-LFRECSHYCELVSTPEQIPQV 140
Cdd:PRK07524 62 SGKPGVCFIITGPGMTNIATAMGQAYADSIPMLVISSvnRRASLGKGRGKLHELPDQRaMVAGVAAFSHTLMSAEDLPEV 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 141 LAIAMrkAVINRG----------VSVVVLPGDVALKAAPESASshwyhaplpQVTPAEEELKKLAQLLRYSSNIALMCGS 210
Cdd:PRK07524 142 LARAF--AVFDSArprpvhieipLDVLAAPADHLLPAPPTRPA---------RPGPAPAALAQAAERLAAARRPLILAGG 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 211 GCAGAHKELVDFAAKLKAPIVHALRGKEHVEYDNPYDVGMTGLIgfSSGFHTMMNADTLVLLGTQF-------PYRAFYP 283
Cdd:PRK07524 211 GALAAAAALRALAERLDAPVALTINAKGLLPAGHPLLLGASQSL--PAVRALIAEADVVLAVGTELgetdydvYFDGGFP 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 284 TDAKIIQIDINPGSIGAHSKVDMALVGDIKSTLSALMPHLEEKTDRKflDKALEHYRDARKgldDLAKPSDKTIHPQ-YL 362
Cdd:PRK07524 289 LPGELIRIDIDPDQLARNYPPALALVGDARAALEALLARLPGQAAAA--DWGAARVAALRQ---ALRAEWDPLTAAQvAL 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 363 AQRISHyADDDAIFTCDvGTPTVWAAR-YLQMNGKRRLL-GSFNHGSMANAMPQAIGAKATAPDRQVVAMCGDGGFSMLM 440
Cdd:PRK07524 364 LDTILA-ALPDAIFVGD-STQPVYAGNlYFDADAPRRWFnASTGYGTLGYGLPAAIGAALGAPERPVVCLVGDGGLQFTL 441
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 441 GDFLSLAQMKLPVKIVIFNNSVLGFVAMEMKAGGYLTDGTELHATNFARIAEACGIKGIRVESASEVDEALQTAFATDGP 520
Cdd:PRK07524 442 PELASAVEADLPLIVLLWNNDGYGEIRRYMVARDIEPVGVDPYTPDFIALARAFGCAAERVADLEQLQAALRAAFARPGP 521
|
....*...
gi 640683833 521 VLVDVVVA 528
Cdd:PRK07524 522 TLIEVDQA 529
|
|
| PRK11269 |
PRK11269 |
glyoxylate carboligase; Provisional |
1-538 |
2.27e-38 |
|
glyoxylate carboligase; Provisional
Pssm-ID: 183066 [Multi-domain] Cd Length: 591 Bit Score: 148.97 E-value: 2.27e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 1 MKQTVAAYIAKTLEQAGVKRIWGVTGDSLNGLSDSLNRMGTIDWMPTRHEEVAAFAAGAEAQLT-GELAVCAGSCGPGNL 79
Cdd:PRK11269 2 AKMRAVDAAVLVLEKEGVTTAFGVPGAAINPFYSAMRKHGGIRHILARHVEGASHMAEGYTRATaGNIGVCIGTSGPAGT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 80 HLINGLFDCHRNHVPVLAIAAHIPSSEIGSGYFQETHPQELFRECSHYCELVSTPEQIPQVLAIAMRKAVINRGVSVVV- 158
Cdd:PRK11269 82 DMITGLYSASADSIPILCITGQAPRARLHKEDFQAVDIESIAKPVTKWAVTVREPALVPRVFQQAFHLMRSGRPGPVLId 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 159 LPGDVALKAAPESASSHwyhAPLP--QVTPAEEELKKLAQLLRYSSNIALMCGSGC--AGAHKELVDFAAKLKAPIVHAL 234
Cdd:PRK11269 162 LPFDVQVAEIEFDPDTY---EPLPvyKPAATRAQIEKALEMLNAAERPLIVAGGGVinADASDLLVEFAELTGVPVIPTL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 235 RGKEHVEYDNPYDVGMTGL-IGFSSGFHTMMNADTLVLLGTQFPYR-----AFYPTDAKIIQIDINPGSIGAHSKVDMAL 308
Cdd:PRK11269 239 MGWGAIPDDHPLMAGMVGLqTSHRYGNATLLASDFVLGIGNRWANRhtgsvEVYTKGRKFVHVDIEPTQIGRVFGPDLGI 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 309 VGDIKSTLSALmphLEEKTDRKFLDKaLEHYRD------ARKGLddLAKPSDKT---IHPQYLAQRISHYADDDAIFTCD 379
Cdd:PRK11269 319 VSDAKAALELL---VEVAREWKAAGR-LPDRSAwvadcqERKRT--LLRKTHFDnvpIKPQRVYEEMNKAFGRDTCYVST 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 380 VGTPTVWAARYLQMNGKRRLLGSFNHGSMANAMPQAIGAKATAPDRQVVAMCGDGGFSMLMGDFLSLAQMKLPVKIVIFN 459
Cdd:PRK11269 393 IGLSQIAAAQFLHVYKPRHWINCGQAGPLGWTIPAALGVRAADPDRNVVALSGDYDFQFLIEELAVGAQFNLPYIHVLVN 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 460 NSVLGFV-----AMEM--------------KAGGYLTDgtelhatnFARIAEACGIKGIRVESASEVDEALQTAFA---- 516
Cdd:PRK11269 473 NAYLGLIrqaqrAFDMdycvqlafeninspELNGYGVD--------HVKVAEGLGCKAIRVFKPEDIAPALEQAKAlmae 544
|
570 580
....*....|....*....|...
gi 640683833 517 TDGPVLVDVVVASEE-LAMPPQI 538
Cdd:PRK11269 545 FRVPVVVEVILERVTnISMGTEI 567
|
|
| TPP_enzyme_M |
pfam00205 |
Thiamine pyrophosphate enzyme, central domain; The central domain of TPP enzymes contains a ... |
191-319 |
1.56e-37 |
|
Thiamine pyrophosphate enzyme, central domain; The central domain of TPP enzymes contains a 2-fold Rossman fold.
Pssm-ID: 425523 [Multi-domain] Cd Length: 137 Bit Score: 135.38 E-value: 1.56e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 191 LKKLAQLLRYSSNIALMCGSGC--AGAHKELVDFAAKLKAPIVHALRGKEHVEYDNPYDVGMTGLIGFSSGFHTMMNADT 268
Cdd:pfam00205 1 IEKAAELLKKAKRPVILAGGGVrrSGASEELRELAEKLGIPVVTTLMGKGAFPEDHPLYLGMLGMHGTPAANEALEEADL 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 640683833 269 LVLLGTQF-------PYRAFYPtDAKIIQIDINPGSIGAHSKVDMALVGDIKSTLSAL 319
Cdd:pfam00205 81 VLAVGARFddirttgKLPEFAP-DAKIIHIDIDPAEIGKNYPVDVPIVGDAKETLEAL 137
|
|
| PRK05858 |
PRK05858 |
acetolactate synthase; |
9-526 |
1.76e-37 |
|
acetolactate synthase;
Pssm-ID: 235629 [Multi-domain] Cd Length: 542 Bit Score: 146.02 E-value: 1.76e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 9 IAKTLEQAGVKRIWGVTGDSLNGLSDSLNRMGtIDWMPTRHEEVAAFAAGAEAQLTGELAVCAGSCGPGNLHLINGLFDC 88
Cdd:PRK05858 11 AARRLKAHGVDTMFTLSGGHLFPLYDGAREEG-IRLIDVRHEQTAAFAAEAWAKLTRVPGVAVLTAGPGVTNGMSAMAAA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 89 HRNHVPVLAIAAHIPSSEIGSGYFQETHPQELFRECSHYCELVSTPEQIPQVLAIAMRKAVI-NRGVSVVVLPGDVALKA 167
Cdd:PRK05858 90 QFNQSPLVVLGGRAPALRWGMGSLQEIDHVPFVAPVTKFAATAQSAENAGRLVDQALQAAVTpHRGPVFVDFPMDHAFSM 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 168 APESASSHWYHAPLPQVTPAEEELKKLAQLLRYSSNIALMCGSGCAGAHKE--LVDFAAKLKAPIVHALRGKEHVEYDNP 245
Cdd:PRK05858 170 ADDDGRPGALTELPAGPTPDPDALARAAGLLAEAQRPVIMAGTDVWWGHAEaaLLRLAEELGIPVLMNGMGRGVVPADHP 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 246 ydvgmtglIGFSSGFHTMM-NADTLVLLGTQFPYR---AFYPTDAKIIQIDINPGSIGAHSKVDMALVGDIKSTLSALMP 321
Cdd:PRK05858 250 --------LAFSRARGKALgEADVVLVVGVPMDFRlgfGVFGGTAQLVHVDDAPPQRAHHRPVAAGLYGDLSAILSALAG 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 322 HLEEKTDRKFLDKALEHYRDARKGLDDLAKPSDKT-IHPQYLAQRISHYADDDAIFTCDVGTPTVWAARYLQMNGKRRLL 400
Cdd:PRK05858 322 AGGDRTDHQGWIEELRTAETAARARDAAELADDRDpIHPMRVYGELAPLLDRDAIVIGDGGDFVSYAGRYIDPYRPGCWL 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 401 GSFNHGSMANAMPQAIGAKATAPDRQVVAMCGDG--GFSMLmgDFLSLAQMKLPVKIVIFNNSVLGFVAMEMKA-GGYLT 477
Cdd:PRK05858 402 DPGPFGCLGTGPGYALAARLARPSRQVVLLQGDGafGFSLM--DVDTLVRHNLPVVSVIGNNGIWGLEKHPMEAlYGYDV 479
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 640683833 478 DGTELHATNFARIAEACGIKGIRVESASEVDEALQTAFATDGPVLVDVV 526
Cdd:PRK05858 480 AADLRPGTRYDEVVRALGGHGELVTVPAELGPALERAFASGVPYLVNVL 528
|
|
| TPP_enzyme_N |
pfam02776 |
Thiamine pyrophosphate enzyme, N-terminal TPP binding domain; |
5-170 |
7.64e-37 |
|
Thiamine pyrophosphate enzyme, N-terminal TPP binding domain;
Pssm-ID: 460690 [Multi-domain] Cd Length: 169 Bit Score: 134.67 E-value: 7.64e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 5 VAAYIAKTLEQAGVKRIWGVTGDSLNGLSDSLNRMGTIDWMPTRHEEVAAFAAGAEAQLTGELAVCAGSCGPGNLHLING 84
Cdd:pfam02776 1 GAEALADVLKALGVDTVFGVPGGHILPLLDALAKSPGIRYVLTRHEQGAAFAADGYARATGKPGVVLVTSGPGATNALTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 85 LFDCHRNHVPVLAIAAHIPSSEIGSGYFQ-ETHPQELFRECSHYCELVSTPEQIPQVLAIAMRKAVINR-GVSVVVLPGD 162
Cdd:pfam02776 81 LANAYVDSVPLLVISGQRPRSLVGRGALQqELDQLALFRPVTKWAVRVTSADEIPEVLRRAFRAALSGRpGPVYLEIPLD 160
|
....*...
gi 640683833 163 VALKAAPE 170
Cdd:pfam02776 161 VLLEEVDE 168
|
|
| TPP_ALS |
cd02010 |
Thiamine pyrophosphate (TPP) family, Acetolactate synthase (ALS) subfamily, TPP-binding module; ... |
359-527 |
9.29e-33 |
|
Thiamine pyrophosphate (TPP) family, Acetolactate synthase (ALS) subfamily, TPP-binding module; composed of proteins similar to Klebsiella pneumoniae ALS, a catabolic enzyme required for butanediol fermentation. ALS catalyzes the conversion of 2 molecules of pyruvate to acetolactate and carbon dioxide. ALS does not contain FAD, and requires TPP and a divalent metal cation for activity.
Pssm-ID: 238968 [Multi-domain] Cd Length: 177 Bit Score: 123.55 E-value: 9.29e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 359 PQYLAQRISHYADDDAIFTCDVGTPTVWAARYLQMNGKRRLLGSFNHGSMANAMPQAIGAKATAPDRQVVAMCGDGGFSM 438
Cdd:cd02010 1 PQRIVHDLRAVMGDDDIVLLDVGAHKIWMARYYRTYAPNTCLISNGLATMGVALPGAIGAKLVYPDRKVVAVSGDGGFMM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 439 LMGDFLSLAQMKLPVKIVIFNNSVLGFVAMEMKAGGYLTDGTELHATNFARIAEACGIKGIRVESASEVDEALQTAFATD 518
Cdd:cd02010 81 NSQELETAVRLKIPLVVLIWNDNGYGLIKWKQEKEYGRDSGVDFGNPDFVKYAESFGAKGYRIESADDLLPVLERALAAD 160
|
....*....
gi 640683833 519 GPVLVDVVV 527
Cdd:cd02010 161 GVHVIDCPV 169
|
|
| TPP_BZL_OCoD_HPCL |
cd02004 |
Thiamine pyrophosphate (TPP) family, BZL_OCoD_HPCL subfamily, TPP-binding module; composed of ... |
359-528 |
3.22e-32 |
|
Thiamine pyrophosphate (TPP) family, BZL_OCoD_HPCL subfamily, TPP-binding module; composed of proteins similar to benzaldehyde lyase (BZL), oxalyl-CoA decarboxylase (OCoD) and 2-hydroxyphytanoyl-CoA lyase (2-HPCL). Pseudomonas fluorescens biovar I BZL cleaves the acyloin linkage of benzoin producing 2 molecules of benzaldehyde and enabling the Pseudomonas to grow on benzoin as the sole carbon and energy source. OCoD has a role in the detoxification of oxalate, catalyzing the decarboxylation of oxalyl-CoA to formate. 2-HPCL is a peroxisomal enzyme which plays a role in the alpha-oxidation of 3-methyl-branched fatty acids, catalyzing the cleavage of 2-hydroxy-3-methylacyl-CoA into formyl-CoA and a 2-methyl-branched fatty aldehyde. All these enzymes depend on Mg2+ and TPP for activity.
Pssm-ID: 238962 [Multi-domain] Cd Length: 172 Bit Score: 121.87 E-value: 3.22e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 359 PQYLAQRISHYADDDAIFTCDVGTPTVWAARYLQMNGKRRLLGSFNHGSMANAMPQAIGAKATAPDRQVVAMCGDGGFSM 438
Cdd:cd02004 1 PYRVLHELQEALPDDAIIVSDGGNTMDWARYILRPRKPRHRLDAGTFGTLGVGLGYAIAAALARPDKRVVLVEGDGAFGF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 439 LMGDFLSLAQMKLPVKIVIFNNSVLGFVAMEM--KAGGYLTDGTELHATNFARIAEACGIKGIRVESASEVDEALQTAFA 516
Cdd:cd02004 81 SGMELETAVRYNLPIVVVVGNNGGWYQGLDGQqlSYGLGLPVTTLLPDTRYDLVAEAFGGKGELVTTPEELKPALKRALA 160
|
170
....*....|..
gi 640683833 517 TDGPVLVDVVVA 528
Cdd:cd02004 161 SGKPALINVIID 172
|
|
| PDC1 |
COG3961 |
TPP-dependent 2-oxoacid decarboxylase, includes indolepyruvate decarboxylase [Carbohydrate ... |
1-539 |
2.62e-30 |
|
TPP-dependent 2-oxoacid decarboxylase, includes indolepyruvate decarboxylase [Carbohydrate transport and metabolism, Coenzyme transport and metabolism, General function prediction only]; TPP-dependent 2-oxoacid decarboxylase, includes indolepyruvate decarboxylase is part of the Pathway/BioSystem: Pyruvate oxidation
Pssm-ID: 443161 [Multi-domain] Cd Length: 545 Bit Score: 124.89 E-value: 2.62e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 1 MKQTVAAYIAKTLEQAGVKRIWGVTGDSLNGLSDSLNRMGTIDWMPTRHeevaafaagaeaqltgELavCAGSC------ 74
Cdd:COG3961 3 MTYTVGDYLLDRLAELGIRHIFGVPGDYNLPFLDAIEAHPGIRWVGCCN----------------EL--NAGYAadgyar 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 75 -----------GPGNLHLINGLFDCHRNHVPVLAIAAhIPSSEI-----------GSGYFqeTHPQELFRECSHYCELVs 132
Cdd:COG3961 65 vnglgalvttyGVGELSAINGIAGAYAERVPVVHIVG-APGTRAqrrgpllhhtlGDGDF--DHFLRMFEEVTVAQAVL- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 133 TPE----QIPQVLAIAMRKaviNRGVsVVVLPGDVAlkAAPESASSHWYHAPLPQVTPA--EEELKKLAQLLRYSSNIAL 206
Cdd:COG3961 141 TPEnaaaEIDRVLAAALRE---KRPV-YIELPRDVA--DAPIEPPEAPLPLPPPASDPAalAAAVAAAAERLAKAKRPVI 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 207 MCGSGCA--GAHKELVDFAAKLKAPIVHALRGKEHVEYDNPYDVGM-TGLIGFSSGFHTMMNADTLVLLGTQFpyrafyp 283
Cdd:COG3961 215 LAGVEVHrfGLQEELLALAEKTGIPVATTLLGKSVLDESHPQFIGTyAGAASSPEVREYVENADCVLCLGVVF------- 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 284 TD-------AKIIQ---IDINPG--SIGAH--SKVDMAlvgDIKSTLSALMPHLEEktdrkfldkaleHYRDARKGLDDL 349
Cdd:COG3961 288 TDtntggftAQLDPertIDIQPDsvRVGGHiyPGVSLA---DFLEALAELLKKRSA------------PLPAPAPPPPPP 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 350 AKPSDKTIHPQYLAQRISHYADDDAIFTCDVGTPtVWAARYLQMNGKRRLLGSFNHGSMANAMPQAIGAKATAPDRQVVA 429
Cdd:COG3961 353 PAAPDAPLTQDRLWQRLQAFLDPGDIVVADTGTS-LFGAADLRLPEGATFIAQPLWGSIGYTLPAALGAALAAPDRRVIL 431
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 430 MCGDGGFsMLMGdfLSLAQM---KLPVKIVIFNNsvlgfvamemkaGGYLT-------DGT--ELHATNFARIAEACG-- 495
Cdd:COG3961 432 LVGDGAF-QLTA--QELSTMlryGLKPIIFVLNN------------DGYTIeraihgpDGPynDIANWDYAKLPEAFGgg 496
|
570 580 590 600
....*....|....*....|....*....|....*....|....*.
gi 640683833 496 -IKGIRVESASEVDEALQTAFA-TDGPVLVDVVVAseELAMPPQIK 539
Cdd:COG3961 497 nALGFRVTTEGELEEALAAAEAnTDRLTLIEVVLD--KMDAPPLLK 540
|
|
| TPP_Xsc_like |
cd02013 |
Thiamine pyrophosphate (TPP) family, Xsc-like subfamily, TPP-binding module; composed of ... |
357-535 |
3.52e-29 |
|
Thiamine pyrophosphate (TPP) family, Xsc-like subfamily, TPP-binding module; composed of proteins similar to Alcaligenes defragrans sulfoacetaldehyde acetyltransferase (Xsc). Xsc plays a key role in the degradation of taurine, catalyzing the desulfonation of 2-sulfoacetaldehyde into sulfite and acetyl phosphate. This enzyme requires TPP and divalent metal ions for activity.
Pssm-ID: 238971 [Multi-domain] Cd Length: 196 Bit Score: 114.14 E-value: 3.52e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 357 IHPQYLAQRISHYADDDAIFTCDVGTPTVWAARYLQMNGKRRLLGSFNHGSMANAMPQAIGAKATAPDRQVVAMCGDGGF 436
Cdd:cd02013 4 MHPRQVLRELEKAMPEDAIVSTDIGNICSVANSYLRFEKPRSFIAPLSFGNCGYALPAIIGAKAAAPDRPVVAIAGDGAW 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 437 SMLMGDFLSLAQMKLPVKIVIFNNSVLGfvaMEMKaggYLTD-------GTELHATNFARIAEACGIKGIRVESASEVDE 509
Cdd:cd02013 84 GMSMMEIMTAVRHKLPVTAVVFRNRQWG---AEKK---NQVDfynnrfvGTELESESFAKIAEACGAKGITVDKPEDVGP 157
|
170 180
....*....|....*....|....*...
gi 640683833 510 ALQTAFA--TDGPVLVDVVVASEELAMP 535
Cdd:cd02013 158 ALQKAIAmmAEGKTTVIEIVCDQELGDP 185
|
|
| PRK07092 |
PRK07092 |
benzoylformate decarboxylase; Reviewed |
78-528 |
1.25e-28 |
|
benzoylformate decarboxylase; Reviewed
Pssm-ID: 235931 [Multi-domain] Cd Length: 530 Bit Score: 119.67 E-value: 1.25e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 78 NLHLING-------LFDCHRNHVPVLAIAAHIPSSEIGSGYF-QETHPQELFRECSHY-CElVSTPEQIPQVLA----IA 144
Cdd:PRK07092 78 NLHSAAGvgnamgnLFTAFKNHTPLVITAGQQARSILPFEPFlAAVQAAELPKPYVKWsIE-PARAEDVPAAIArayhIA 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 145 MRKAvinRGVSVVVLPGDVALKAAPESASSHWYHAplpqVTPAEEELKKLAQLLRYSSNIALMCGSGC--AGAHKELVDF 222
Cdd:PRK07092 157 MQPP---RGPVFVSIPYDDWDQPAEPLPARTVSSA----VRPDPAALARLGDALDAARRPALVVGPAVdrAGAWDDAVRL 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 223 AAKLKAPIVHAlrgkehveydnPydvgMTGLIGFSS------GFHTMMNA---------DTLVLLGT------QFPYRAF 281
Cdd:PRK07092 230 AERHRAPVWVA-----------P----MSGRCSFPEdhplfaGFLPASREkisalldghDLVLVIGApvftyhVEGPGPH 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 282 YPTDAKIIQIDINPGsIGAHSKVDMALVGDIKSTLSALmphleektdrkfLDKALEHYRDARKGLDDLAKPSDKT--IHP 359
Cdd:PRK07092 295 LPEGAELVQLTDDPG-EAAWAPMGDAIVGDIRLALRDL------------LALLPPSARPAPPARPMPPPAPAPGepLSV 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 360 QYLAQRISHYADDDAIFTCDV--GTPTVWaaRYLQMNGKrrllGSF---NHGSMANAMPQAIGAKATAPDRQVVAMCGDG 434
Cdd:PRK07092 362 AFVLQTLAALRPADAIVVEEApsTRPAMQ--EHLPMRRQ----GSFytmASGGLGYGLPAAVGVALAQPGRRVIGLIGDG 435
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 435 GFSMLMGDFLSLAQMKLPVKIVIFNNSvlGFVAME-----MKAGGylTDGTELHATNFARIAEACGIKGIRVESASEVDE 509
Cdd:PRK07092 436 SAMYSIQALWSAAQLKLPVTFVILNNG--RYGALRwfapvFGVRD--VPGLDLPGLDFVALARGYGCEAVRVSDAAELAD 511
|
490
....*....|....*....
gi 640683833 510 ALQTAFATDGPVLVDVVVA 528
Cdd:PRK07092 512 ALARALAADGPVLVEVEVA 530
|
|
| IolD |
COG3962 |
TPP-dependent trihydroxycyclohexane-1,2-dione (THcHDO) dehydratase, myo-inositol metabolism ... |
69-527 |
2.42e-28 |
|
TPP-dependent trihydroxycyclohexane-1,2-dione (THcHDO) dehydratase, myo-inositol metabolism [Carbohydrate transport and metabolism];
Pssm-ID: 443162 [Multi-domain] Cd Length: 622 Bit Score: 119.46 E-value: 2.42e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 69 VCAGSCGPGNLHLINGLFDCHRNHVPVLAIAAHIPSSEIGSGYFQET-HPQEL-------FRECSHYCELVSTPEQIPQV 140
Cdd:COG3962 87 ACTSSIGPGATNMVTAAALATANRLPVLLLPGDTFATRQPDPVLQQLeHFHDPtisvndaFRPVSRYWDRITRPEQLMSA 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 141 LAIAMRkaVI----NRGVSVVVLPGDVALKA--APES--ASSHWYhapLPQVTPAEEELKKLAQLLRYSSNIALMCGSGC 212
Cdd:COG3962 167 LPRAMR--VLtdpaETGAVTLALPQDVQAEAydYPESffAKRVHR---IRRPPPDPAELARAVELIRAAKRPLIIAGGGV 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 213 --AGAHKELVDFAAKLKAPIVHALRGKEHVEYDNPYDVGMTGLIGFSSGFHTMMNADTLVLLGTQF------PYRAFYPT 284
Cdd:COG3962 242 rySEATEALRAFAEATGIPVAETQAGKGALPWDHPLNLGGIGVTGTLAANALAAEADLVIGVGTRLqdfttgSKTLFANP 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 285 DAKIIQIDINPGSIGAHSKVdmALVGDIKSTLSALMPHLEE-KTDRKFLDKALEHYRDARKGLDDLAKPSDKTIHPQylA 363
Cdd:COG3962 322 DVRFVNINVARFDAYKHDAL--PVVADAREGLEALTEALAGwRYPAAWTDEAAELKAEWDAEVDRLYAPTNGGLPTQ--A 397
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 364 QRI---SHYADDDAIFTCDVGTP-----TVWAARYlqmngkrrlLGSFN--HG--SMANAMPQAIGAKATAPDRQVVAMC 431
Cdd:COG3962 398 QVIgavNEAAGPDDIVVCAAGSLpgdlhKLWRTRD---------PGTYHveYGysCMGYEIAGGLGVKLAEPDREVYVMV 468
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 432 GDGGFSMLMGDFLSLAQMKLPVKIVIFNNSvlGFV---AMEMKAGG--------------YLTDGtELHATNFARIAEAC 494
Cdd:COG3962 469 GDGSYLMLNSELVTSVQEGKKIIVVLLDNH--GFGcinRLQMSTGSqsfgtelrdrdtetGRLDG-GLLPVDFAANAASL 545
|
490 500 510
....*....|....*....|....*....|...
gi 640683833 495 GIKGIRVESASEVDEALQTAFATDGPVLVDVVV 527
Cdd:COG3962 546 GAKAYRVTTIAELRAALERAKAADRTTVIVIKT 578
|
|
| TPP_BFDC |
cd02002 |
Thiamine pyrophosphate (TPP) family, BFDC subfamily, TPP-binding module; composed of proteins ... |
357-527 |
2.79e-27 |
|
Thiamine pyrophosphate (TPP) family, BFDC subfamily, TPP-binding module; composed of proteins similar to Pseudomonas putida benzoylformate decarboxylase (BFDC). P. putida BFDC plays a role in the mandelate pathway, catalyzing the conversion of benzoylformate to benzaldehyde and carbon dioxide. This enzyme is dependent on TPP and a divalent metal cation as cofactors.
Pssm-ID: 238960 [Multi-domain] Cd Length: 178 Bit Score: 108.45 E-value: 2.79e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 357 IHPQYLAQRISHYADDDAIFTCDVGTPTVWAARYLQMNGKRRLLGSfNHGSMANAMPQAIGAKATAPDRQVVAMCGDGGF 436
Cdd:cd02002 1 LTPEYLAAALAAALPEDAIIVDEAVTNGLPLRDQLPLTRPGSYFTL-RGGGLGWGLPAAVGAALANPDRKVVAIIGDGSF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 437 SMLMGDFLSLAQMKLPVKIVIFNNSVLGFVAMEMKAGGYLTDGTE------LH--ATNFARIAEACGIKGIRVESASEVD 508
Cdd:cd02002 80 MYTIQALWTAARYGLPVTVVILNNRGYGALRSFLKRVGPEGPGENapdgldLLdpGIDFAAIAKAFGVEAERVETPEELD 159
|
170
....*....|....*....
gi 640683833 509 EALQTAFATDGPVLVDVVV 527
Cdd:cd02002 160 EALREALAEGGPALIEVVV 178
|
|
| TPP_PYR_POX_like |
cd07035 |
Pyrimidine (PYR) binding domain of POX and related proteins; Thiamine pyrophosphate (TPP ... |
8-160 |
2.85e-25 |
|
Pyrimidine (PYR) binding domain of POX and related proteins; Thiamine pyrophosphate (TPP family), pyrimidine (PYR) binding domain of pyruvate oxidase (POX) and related protiens subfamily. The PYR domain is found in many key metabolic enzymes which use TPP (also known as thiamine diphosphate) as a cofactor. TPP binds in the cleft formed by a PYR domain and a PP domain. The PYR domain, binds the aminopyrimidine ring of TPP, the PP domain binds the diphosphate residue. A polar interaction between the conserved glutamate of the PYR domain and the N1' of the TPP aminopyrimidine ring is shared by most TPP-dependent enzymes, and participates in the activation of TPP. For glyoxylate carboligase, which belongs to this subfamily, but lacks this conserved glutamate, the rate of the initial TPP activation step is reduced but the ensuing steps of the enzymic reaction proceed efficiently. The PYR and PP domains have a common fold, but do not share strong sequence conservation. The PP domain is not included in this sub-family. Most TPP-dependent enzymes have the PYR and PP domains on the same subunit although these domains can be alternatively arranged in the primary structure. TPP-dependent enzymes are multisubunit proteins, the smallest catalytic unit being a dimer-of-active sites, for many the active sites lie between PP and PYR domains on different subunits. POX decarboxylates pyruvate, producing hydrogen peroxide and the energy-storage metabolite acetylphosphate. This subfamily includes pyruvate decarboxylase (PDC) and indolepyruvate decarboxylase (IPDC). PDC catalyzes the conversion of pyruvate to acetaldehyde and CO2 in alcoholic fermentation. IPDC plays a role in the indole-3-pyruvic acid (IPA) pathway in plants and various plant-associated bacteria, it catalyzes the decarboxylation of IPA to IAA. This subfamily also includes the large catalytic subunit of acetohydroxyacid synthase (AHAS). AHAS catalyzes the condensation of two molecules of pyruvate to give the acetohydroxyacid, 2-acetolactate, a precursor of the branched chain amino acids, valine and leucine. AHAS also catalyzes the condensation of pyruvate and 2-ketobutyrate to form 2-aceto-2-hydroxybutyrate in isoleucine biosynthesis. Methanococcus jannaschii sulfopyruvate decarboxylase (MjComDE) and phosphonopyruvate decarboxylase (PpyrDc) also belong to this subfamily. PpyrDc is a homotrimeric enzyme having the PP and PYR domains tandemly arranged on the same subunit. It functions in the biosynthesis of C-P compounds such as bialaphos tripeptide in Streptomyces hygroscopicus. MjComDE is a dodecamer having the PYR and PP domains on different subunits, it has six alpha (PYR/ComD) subunits and six beta (PP/ComE) subunits. MjComDE catalyzes the decarboxylation of sulfopyruvic acid to sulfoacetaldehyde in the coenzyme M pathway.
Pssm-ID: 132918 [Multi-domain] Cd Length: 155 Bit Score: 101.84 E-value: 2.85e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 8 YIAKTLEQAGVKRIWGVTGDSLNGLSDSLNRMGtIDWMPTRHEEVAAFAAGAEAQLTGELAVCAGSCGPGNLHLINGLFD 87
Cdd:cd07035 2 ALVEALKAEGVDHVFGVPGGAILPLLDALARSG-IRYILVRHEQGAVGMADGYARATGKPGVVLVTSGPGLTNAVTGLAN 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 640683833 88 CHRNHVPVLAIAAHIPSSEIGSGYFQETHPQELFRECSHYCELVSTPEQIPQVLAIAMRKAVINR-GVSVVVLP 160
Cdd:cd07035 81 AYLDSIPLLVITGQRPTAGEGRGAFQEIDQVALFRPITKWAYRVTSPEEIPEALRRAFRIALSGRpGPVALDLP 154
|
|
| PRK09259 |
PRK09259 |
putative oxalyl-CoA decarboxylase; Validated |
6-528 |
2.55e-19 |
|
putative oxalyl-CoA decarboxylase; Validated
Pssm-ID: 236433 [Multi-domain] Cd Length: 569 Bit Score: 91.59 E-value: 2.55e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 6 AAYIAKTLEQAGVKRIWGVTGDSLNGLSDSLNRMGtIDWMPTRHEEVAAFAAGAEAQLTGELAVCAGSCGPGNLHLINGL 85
Cdd:PRK09259 13 FHLVIDALKLNGIDTIYGVVGIPITDLARLAQAEG-IRYIGFRHEQSAGNAAAAAGFLTQKPGVCLTVSAPGFLNGLTAL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 86 FDCHRNHVPVLAIAAhipSSE-----IGSGYFQET--------HPQELFRecshycelVSTPEQIPQVLAIAMRKAVINR 152
Cdd:PRK09259 92 ANATTNCFPMIMISG---SSEreivdLQQGDYEELdqlnaakpFCKAAFR--------VNRAEDIGIGVARAIRTAVSGR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 153 -GVSVVVLPGDV--ALKAAPESASSHWYHA-PLPQVTPAEEELKKLAQLLRYSSN--IALMCGSGCAGAHKELVDFAAKL 226
Cdd:PRK09259 161 pGGVYLDLPAKVlaQTMDADEALTSLVKVVdPAPAQLPAPEAVDRALDLLKKAKRplIILGKGAAYAQADEQIREFVEKT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 227 KAPIVHALRGKEHVEYDNPYDVGmtgligfSSGFHTMMNADTLVLLGTQFPYRAFY---PT---DAKIIQIDINPGSIGA 300
Cdd:PRK09259 241 GIPFLPMSMAKGLLPDTHPQSAA-------AARSLALANADVVLLVGARLNWLLSHgkgKTwgaDKKFIQIDIEPQEIDS 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 301 HSKVDMALVGDIKSTLSALMPHLEE---KTDRKFLDKALEhyrDARKGLDDLAKPSDKTIHPQ--YLAQR-ISHYADD-- 372
Cdd:PRK09259 314 NRPIAAPVVGDIGSVMQALLAGLKQntfKAPAEWLDALAE---RKEKNAAKMAEKLSTDTQPMnfYNALGaIRDVLKEnp 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 373 DAIFTCDvGTPTVWAAR-YLQMNGKRRLLGSFNHGSMANAMPQAIGAkATAPDRQVVAMCGDGGFSMLMGDFLSLAQMKL 451
Cdd:PRK09259 391 DIYLVNE-GANTLDLARnIIDMYKPRHRLDCGTWGVMGIGMGYAIAA-AVETGKPVVAIEGDSAFGFSGMEVETICRYNL 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 452 PVKIVIFNNSvlgfvamemkaGGY------LTDGTELHATNFA------RIAEACGIKGIRVESASEVDEALQTAFATDG 519
Cdd:PRK09259 469 PVTVVIFNNG-----------GIYrgddvnLSGAGDPSPTVLVhharydKMMEAFGGVGYNVTTPDELRHALTEAIASGK 537
|
....*....
gi 640683833 520 PVLVDVVVA 528
Cdd:PRK09259 538 PTLINVVID 546
|
|
| PRK12474 |
PRK12474 |
hypothetical protein; Provisional |
62-527 |
3.34e-18 |
|
hypothetical protein; Provisional
Pssm-ID: 139002 [Multi-domain] Cd Length: 518 Bit Score: 87.62 E-value: 3.34e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 62 QLTGELAVCAGSCGPGnlhLINGLFDCH---RNHVPVLAI-----AAHIP-----SSEIGSgyfqethpqeLFRECSHYC 128
Cdd:PRK12474 64 RIAGKPAVTLLHLGPG---LANGLANLHnarRAASPIVNIvgdhaVEHLQydaplTSDIDG----------FARPVSRWV 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 129 ELVSTPEQIPQVLAIAMRKA-VINRGVSVVVLPGDVALKAAPESAsshwyhAPLPQVTPA---EEELKKLAQLLRYSSNI 204
Cdd:PRK12474 131 HRSASAGAVDSDVARAVQAAqSAPGGIATLIMPADVAWNEAAYAA------QPLRGIGPApvaAETVERIAALLRNGKKS 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 205 ALMC-GSGCAGAHKELVD-FAAKLKAPIV------HALRGKEHVEYDNpydVGMTGLIGfssgfhTMM--NADTLVLLGT 274
Cdd:PRK12474 205 ALLLrGSALRGAPLEAAGrIQAKTGVRLYcdtfapRIERGAGRVPIER---IPYFHEQI------TAFlkDVEQLVLVGA 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 275 QFPYRAF-YPTdakiiqidiNPGSIGAHSKVDMALVGdikstlsalmPHLEEKTDRKFLDKALEHYRD--ARKGLDDLAK 351
Cdd:PRK12474 276 KPPVSFFaYPG---------KPSWGAPPGCEIVYLAQ----------PDEDLAQALQDLADAVDAPAEpaARTPLALPAL 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 352 PSDKtIHPQYLAQRISHYADDDAIFTCDVGTPTVW------AAR---YLQMNGkrrllgsfnhGSMANAMPQAIGAKATA 422
Cdd:PRK12474 337 PKGA-LNSLGVAQLIAHRTPDQAIYADEALTSGLFfdmsydRARphtHLPLTG----------GSIGQGLPLAAGAAVAA 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 423 PDRQVVAMCGDGGFSMLMGDFLSLAQMKLPVKIVIFNNSVLGFVAMEMKAGGYLTDGT------ELH--ATNFARIAEAC 494
Cdd:PRK12474 406 PDRKVVCPQGDGGAAYTMQALWTMARENLDVTVVIFANRSYAILNGELQRVGAQGAGRnalsmlDLHnpELNWMKIAEGL 485
|
490 500 510
....*....|....*....|....*....|...
gi 640683833 495 GIKGIRVESASEVDEALQTAFATDGPVLVDVVV 527
Cdd:PRK12474 486 GVEASRATTAEEFSAQYAAAMAQRGPRLIEAMI 518
|
|
| PRK07586 |
PRK07586 |
acetolactate synthase large subunit; |
359-527 |
1.16e-17 |
|
acetolactate synthase large subunit;
Pssm-ID: 236063 [Multi-domain] Cd Length: 514 Bit Score: 86.05 E-value: 1.16e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 359 PQYLAQRISHYADDDAIF-----TCDVG--TPTVWAAR--YLQMNGkrrllgsfnhGSMANAMPQAIGAKATAPDRQVVA 429
Cdd:PRK07586 339 PEAIAQVIAALLPENAIVvdesiTSGRGffPATAGAAPhdWLTLTG----------GAIGQGLPLATGAAVACPDRKVLA 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 430 MCGDGGFSMLMGDFLSLAQMKLPVKIVIFNNSVLGFVAMEMKAGGYLTDG------TELH--ATNFARIAEACGIKGIRV 501
Cdd:PRK07586 409 LQGDGSAMYTIQALWTQARENLDVTTVIFANRAYAILRGELARVGAGNPGpraldmLDLDdpDLDWVALAEGMGVPARRV 488
|
170 180
....*....|....*....|....*.
gi 640683833 502 ESASEVDEALQTAFATDGPVLVDVVV 527
Cdd:PRK07586 489 TTAEEFADALAAALAEPGPHLIEAVV 514
|
|
| TPP_PDC_IPDC |
cd02005 |
Thiamine pyrophosphate (TPP) family, PDC_IPDC subfamily, TPP-binding module; composed of ... |
361-532 |
8.61e-17 |
|
Thiamine pyrophosphate (TPP) family, PDC_IPDC subfamily, TPP-binding module; composed of proteins similar to pyruvate decarboxylase (PDC) and indolepyruvate decarboxylase (IPDC). PDC, a key enzyme in alcoholic fermentation, catalyzes the conversion of pyruvate to acetaldehyde and CO2. It is able to utilize other 2-oxo acids as substrates. In plants and various plant-associated bacteria, IPDC plays a role in the indole-3-pyruvic acid (IPA) pathway, a tryptophan-dependent biosynthetic route to indole-3-acetaldehyde (IAA). IPDC catalyzes the decarboxylation of IPA to IAA. Both PDC and IPDC depend on TPP and Mg2+ as cofactors.
Pssm-ID: 238963 [Multi-domain] Cd Length: 183 Bit Score: 78.34 E-value: 8.61e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 361 YLAQRISHYADDDAIFTCDVGTPTvWAARYLQMNGKRRLLGSFNHGSMANAMPQAIGAKATAPDRQVVAMCGDGGFSMLM 440
Cdd:cd02005 6 RLWQQVQNFLKPNDILVAETGTSW-FGALDLKLPKGTRFISQPLWGSIGYSVPAALGAALAAPDRRVILLVGDGSFQMTV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 441 GDFLSLAQMKLPVKIVIFNNSvlgfvamemkagGYLTDgTELH---------AT-NFARIAEACG----IKGIRVESASE 506
Cdd:cd02005 85 QELSTMIRYGLNPIIFLINND------------GYTIE-RAIHgpeasyndiANwNYTKLPEVFGggggGLSFRVKTEGE 151
|
170 180 190
....*....|....*....|....*....|.
gi 640683833 507 VDEALQTA-FATDGPVLVDVVV----ASEEL 532
Cdd:cd02005 152 LDEALKDAlFNRDKLSLIEVILpkddAPEAL 182
|
|
| TPP_IolD |
cd02003 |
Thiamine pyrophosphate (TPP) family, IolD subfamily, TPP-binding module; composed of proteins ... |
364-525 |
6.41e-15 |
|
Thiamine pyrophosphate (TPP) family, IolD subfamily, TPP-binding module; composed of proteins similar to Rhizobium leguminosarum bv. viciae IolD. IolD plays an important role in myo-inositol catabolism.
Pssm-ID: 238961 [Multi-domain] Cd Length: 205 Bit Score: 73.88 E-value: 6.41e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 364 QRISHYADDDAIFTCDVGTPtvwaARYLQMNGKRRLLGSFN----HGSMANAMPQAIGAKATAPDRQVVAMCGDGGFSML 439
Cdd:cd02003 6 GALNEAIGDDDVVINAAGSL----PGDLHKLWRARTPGGYHleygYSCMGYEIAAGLGAKLAKPDREVYVLVGDGSYLML 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 440 MGDFLSLAQMKLPVKIVIFNNS---VLGFVAMEMKAGGYltdGTELHA--------------TNFARIAEACGIKGIRVE 502
Cdd:cd02003 82 HSEIVTAVQEGLKIIIVLFDNHgfgCINNLQESTGSGSF---GTEFRDrdqesgqldgallpVDFAANARSLGARVEKVK 158
|
170 180
....*....|....*....|...
gi 640683833 503 SASEVDEALQTAFATDGPVLVDV 525
Cdd:cd02003 159 TIEELKAALAKAKASDRTTVIVI 181
|
|
| Ppyr-DeCO2ase |
TIGR03297 |
phosphonopyruvate decarboxylase; This family consists of examples of phosphonopyruvate an ... |
360-536 |
2.49e-14 |
|
phosphonopyruvate decarboxylase; This family consists of examples of phosphonopyruvate an decarboxylase enzyme that produces phosphonoacetaldehyde (Pald), the second step in the biosynthesis phosphonate-containing compounds. Since the preceding enzymate step, PEP phosphomutase (AepX, TIGR02320) favors the substrate PEP energetically, the decarboxylase is required to drive the reaction in the direction of phosphonate production. Pald is a precursor of natural products including antibiotics like bialaphos and phosphonothricin in Streptomyces species, phosphonate-modified molecules such as the polysaccharide B of Bacteroides fragilis, the phosphonolipids of Tetrahymena pyroformis, the glycosylinositolphospholipids of Trypanosoma cruzi. This gene generally occurs in prokaryotic organisms adjacent to the gene for AepX. Most often an aminotansferase (aepZ) is also present which leads to the production of the most common phosphonate compound, 2-aminoethylphosphonate (AEP).
Pssm-ID: 274508 [Multi-domain] Cd Length: 361 Bit Score: 74.70 E-value: 2.49e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 360 QYLAQRISHYADDDAIftcdVGTpTVWAARYLQMNGKRRLLGSFNH----GSMANAMPQAIGAKATAPDRQVVAMCGDGG 435
Cdd:TIGR03297 176 EAIAAILDHLPDNTVI----VST-TGKTSRELYELRDRIGQGHARDfltvGSMGHASQIALGLALARPDQRVVCLDGDGA 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 436 FSMLMGDFLSLAQMKLPVKI-VIFNNSVLGFVamemkaGGYLTDGTELhatNFARIAEACGI-KGIRVESASEVDEALQT 513
Cdd:TIGR03297 251 ALMHMGGLATIGTQGPANLIhVLFNNGAHDSV------GGQPTVSQHL---DFAQIAKACGYaKVYEVSTLEELETALTA 321
|
170 180
....*....|....*....|...
gi 640683833 514 AFATDGPVLVDVVVASEELAMPP 536
Cdd:TIGR03297 322 ASSANGPRLIEVKVRPGSRADLG 344
|
|
| TPP_Gcl |
cd02006 |
Thiamine pyrophosphate (TPP) family, Gcl subfamily, TPP-binding module; composed of proteins ... |
357-527 |
1.93e-13 |
|
Thiamine pyrophosphate (TPP) family, Gcl subfamily, TPP-binding module; composed of proteins similar to Escherichia coli glyoxylate carboligase (Gcl). E. coli glyoxylate carboligase, plays a key role in glyoxylate metabolism where it catalyzes the condensation of two molecules of glyoxylate to give tartronic semialdehyde and carbon dioxide. This enzyme requires TPP, magnesium ion and FAD as cofactors.
Pssm-ID: 238964 [Multi-domain] Cd Length: 202 Bit Score: 69.23 E-value: 1.93e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 357 IHPQYLAQRISHYADDDAIFTCDVGTPTVWAARYLQMNGKRRLLGSFNHGSMANAMPQAIGAKATAPDRQVVAMCGDGGF 436
Cdd:cd02006 8 IKPQRVYEEMNKAFGRDVRYVTTIGLSQIAGAQMLHVYKPRHWINCGQAGPLGWTVPAALGVAAADPDRQVVALSGDYDF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 437 SMLMGDFLSLAQMKLPVKIVIFNNSVLGFVAMEMKA-------------------GGYLTDgtelhatnFARIAEACGIK 497
Cdd:cd02006 88 QFMIEELAVGAQHRIPYIHVLVNNAYLGLIRQAQRAfdmdyqvnlafeninsselGGYGVD--------HVKVAEGLGCK 159
|
170 180 190
....*....|....*....|....*....|....
gi 640683833 498 GIRVESASEVDEALQTAFATDG----PVLVDVVV 527
Cdd:cd02006 160 AIRVTKPEELAAAFEQAKKLMAehrvPVVVEAIL 193
|
|
| TPP_PpyrDC |
cd03371 |
Thiamine pyrophosphate (TPP) family, PpyrDC subfamily, TPP-binding module; composed of ... |
406-533 |
5.83e-12 |
|
Thiamine pyrophosphate (TPP) family, PpyrDC subfamily, TPP-binding module; composed of proteins similar to phosphonopyruvate decarboxylase (PpyrDC) proteins. PpyrDC is a homotrimeric enzyme which functions in the biosynthesis of C-P compounds such as bialaphos tripeptide in Streptomyces hygroscopicus. These proteins require TPP and divalent metal cation cofactors.
Pssm-ID: 239468 [Multi-domain] Cd Length: 188 Bit Score: 64.64 E-value: 5.83e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 406 GSMANAMPQAIGAKATAPDRQVVAMCGDGGFSMLMGDFLSLAQMKLP-VKIVIFNNSVLGFVamemkaGGYLTDGTelhA 484
Cdd:cd03371 48 GSMGHASQIALGIALARPDRKVVCIDGDGAALMHMGGLATIGGLAPAnLIHIVLNNGAHDSV------GGQPTVSF---D 118
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 640683833 485 TNFARIAEACGIKGIR-VESASEVDEALQTAFATDGPVLVDVVVASEELA 533
Cdd:cd03371 119 VSLPAIAKACGYRAVYeVPSLEELVAALAKALAADGPAFIEVKVRPGSRS 168
|
|
| TPP_enzyme_PYR |
cd06586 |
Pyrimidine (PYR) binding domain of thiamine pyrophosphate (TPP)-dependent enzymes; Thiamine ... |
7-161 |
3.54e-11 |
|
Pyrimidine (PYR) binding domain of thiamine pyrophosphate (TPP)-dependent enzymes; Thiamine pyrophosphate (TPP) family, pyrimidine (PYR) binding domain; found in many key metabolic enzymes which use TPP (also known as thiamine diphosphate) as a cofactor. TPP binds in the cleft formed by a PYR domain and a PP domain. The PYR domain, binds the aminopyrimidine ring of TPP, the PP domain binds the diphosphate residue. A polar interaction between the conserved glutamate of the PYR domain and the N1' of the TPP aminopyrimidine ring is shared by most TPP-dependent enzymes, and participates in the activation of TPP. The PYR and PP domains have a common fold, but do not share strong sequence conservation. The PP domain is not included in this group. Most TPP-dependent enzymes have the PYR and PP domains on the same subunit although these domains can be alternatively arranged in the primary structure. In the case of 2-oxoisovalerate dehydrogenase (2OXO), sulfopyruvate decarboxylase (ComDE), and the E1 component of human pyruvate dehydrogenase complex (E1- PDHc) the PYR and PP domains appear on different subunits. TPP-dependent enzymes are multisubunit proteins, the smallest catalytic unit being a dimer-of-active sites. For many of these enzymes the active sites lie between PP and PYR domains on different subunits. However, for the homodimeric enzymes 1-deoxy-D-xylulose 5-phosphate synthase (DXS) and Desulfovibrio africanus pyruvate:ferredoxin oxidoreductase (PFOR), each active site lies at the interface of the PYR and PP domains from the same subunit.
Pssm-ID: 132915 [Multi-domain] Cd Length: 154 Bit Score: 61.59 E-value: 3.54e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 7 AYIAKTLEQAGVKRIWGVTGDSLNGLSDSLNRMGTIDWMPTRHEEVAAFAAGAEAQLTGeLAVCAGSCGPGNLHLINGLF 86
Cdd:cd06586 1 AAFAEVLTAWGVRHVFGYPGDEISSLLDALREGDKRIIDTVIHELGAAGAAAGYARAGG-PPVVIVTSGTGLLNAINGLA 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 640683833 87 DCHRNHVPVLAIAAHIPSSEIGSGYFQETHPQELFRECSHYCELVSTPEQIPQVLAIAMRKAVINRGVSVVVLPG 161
Cdd:cd06586 80 DAAAEHLPVVFLIGARGISAQAKQTFQSMFDLGMYRSIPEANISSPSPAELPAGIDHAIRTAYASQGPVVVRLPR 154
|
|
| TPP_ComE |
cd03372 |
Thiamine pyrophosphate (TPP) family, ComE subfamily, TPP-binding module; composed of proteins ... |
366-527 |
1.09e-08 |
|
Thiamine pyrophosphate (TPP) family, ComE subfamily, TPP-binding module; composed of proteins similar to Methanococcus jannaschii sulfopyruvate decarboxylase beta subunit (ComE). M. jannaschii sulfopyruvate decarboxylase (ComDE) is a dodecamer of six alpha (D) subunits and six (E) beta subunits, which catalyzes the decarboxylation of sulfopyruvic acid to sulfoacetaldehyde in the coenzyme M pathway. ComDE requires TPP and divalent metal cation cofactors.
Pssm-ID: 239469 [Multi-domain] Cd Length: 179 Bit Score: 54.99 E-value: 1.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 366 ISHYADD--DAIFTCDVGTPT--VWAARylqmngkRRLLGSFNHGSMANAMPQAIGAkATAPDRQVVAMCGDGGFSMLMG 441
Cdd:cd03372 5 IKTLIADlkDELVVSNIGFPSkeLYAAG-------DRPLNFYMLGSMGLASSIGLGL-ALAQPRKVIVIDGDGSLLMNLG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 442 DFLSLAQMKLP-VKIVIFNNSVLGFVAMEMKaggYLTDGTELHAtnfarIAEACGIKGIRVESAsevDEALQTAF--ATD 518
Cdd:cd03372 77 ALATIAAEKPKnLIIVVLDNGAYGSTGNQPT---HAGKKTDLEA-----VAKACGLDNVATVAS---EEAFEKAVeqALD 145
|
....*....
gi 640683833 519 GPVLVDVVV 527
Cdd:cd03372 146 GPSFIHVKI 154
|
|
| TPP_ComE_PpyrDC |
cd02001 |
Thiamine pyrophosphate (TPP) family, ComE and PpyrDC subfamily, TPP-binding module; composed ... |
406-523 |
1.82e-07 |
|
Thiamine pyrophosphate (TPP) family, ComE and PpyrDC subfamily, TPP-binding module; composed of proteins similar to sulfopyruvate decarboxylase beta subunit (ComE) and phosphonopyruvate decarboxylase (Ppyr decarboxylase). Methanococcus jannaschii sulfopyruvate decarboxylase (ComDE) is a dodecamer of six alpha (D) subunits and six (E) beta subunits which, catalyzes the decarboxylation of sulfopyruvic acid to sulfoacetaldehyde in the coenzyme M pathway. Ppyr decarboxylase is a homotrimeric enzyme which functions in the biosynthesis of C-P compounds such as bialaphos tripeptide in Streptomyces hygroscopicus. Ppyr decarboxylase and ComDE require TPP and divalent metal cation cofactors.
Pssm-ID: 238959 [Multi-domain] Cd Length: 157 Bit Score: 50.95 E-value: 1.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 406 GSMANAMPQAIGAKATAPdRQVVAMCGDGGFSMLMGDFLSLAQMK-LPVKIVIFNNSVLGfvamemKAGGYLTDGTelhA 484
Cdd:cd02001 42 GSMGLAGSIGLGLALGLS-RKVIVVDGDGSLLMNPGVLLTAGEFTpLNLILVVLDNRAYG------STGGQPTPSS---N 111
|
90 100 110
....*....|....*....|....*....|....*....
gi 640683833 485 TNFARIAEACGIKGIRVESASEVDEALQTAFATDGPVLV 523
Cdd:cd02001 112 VNLEAWAAACGYLVLSAPLLGGLGSEFAGLLATTGPTLL 150
|
|
| PRK06163 |
PRK06163 |
hypothetical protein; Provisional |
406-545 |
8.17e-07 |
|
hypothetical protein; Provisional
Pssm-ID: 235721 [Multi-domain] Cd Length: 202 Bit Score: 49.83 E-value: 8.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 406 GSMANAMPQAIGAKATAPDRQVVAMCGDGGFSMLMGDFLSLAQMKLP-VKIVIFNNSVLGFvamemkAGGYLTDGTelHA 484
Cdd:PRK06163 57 GSMGLAFPIALGVALAQPKRRVIALEGDGSLLMQLGALGTIAALAPKnLTIIVMDNGVYQI------TGGQPTLTS--QT 128
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 640683833 485 TNFARIAEACGIkgirVESASEVDEA-----LQTAFATDGPVLVDVVVASEELAM-----PPQIKLEQAKG 545
Cdd:PRK06163 129 VDVVAIARGAGL----ENSHWAADEAhfealVDQALSGPGPSFIAVRIDDKPGVGtterdPAQIRERFMQG 195
|
|
| TPP_SHCHC_synthase |
cd02009 |
Thiamine pyrophosphate (TPP) family, SHCHC synthase subfamily, TPP-binding module; composed of ... |
415-527 |
9.19e-06 |
|
Thiamine pyrophosphate (TPP) family, SHCHC synthase subfamily, TPP-binding module; composed of proteins similar to Escherichia coli 2-succinyl-6-hydroxyl-2,4-cyclohexadiene-1-carboxylic acid (SHCHC) synthase (also called MenD). SHCHC synthase plays a key role in the menaquinone biosynthetic pathway, converting isochorismate and 2-oxoglutarate to SHCHC, pyruvate and carbon dioxide. The enzyme requires TPP and a divalent metal cation for activity.
Pssm-ID: 238967 [Multi-domain] Cd Length: 175 Bit Score: 46.43 E-value: 9.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 415 AIGAkATAPDRQVVAMCGDggFSML--MGDFLSLAQMKLPVKIVIFNNSvlG---FvamEMKAGGYLTDGTE-----LHA 484
Cdd:cd02009 60 ALGI-ALATDKPTVLLTGD--LSFLhdLNGLLLGKQEPLNLTIVVINNN--GggiF---SLLPQASFEDEFErlfgtPQG 131
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 640683833 485 TNFARIAEACGIKGIRVESASEVDEALQTAFATDGPVLVDVVV 527
Cdd:cd02009 132 LDFEHLAKAYGLEYRRVSSLDELEQALESALAQDGPHVIEVKT 174
|
|
| TPP_E1_PDC_ADC_BCADC |
cd02000 |
Thiamine pyrophosphate (TPP) family, E1 of PDC_ADC_BCADC subfamily, TPP-binding module; ... |
412-527 |
3.56e-05 |
|
Thiamine pyrophosphate (TPP) family, E1 of PDC_ADC_BCADC subfamily, TPP-binding module; composed of proteins similar to the E1 components of the human pyruvate dehydrogenase complex (PDC), the acetoin dehydrogenase complex (ADC) and the branched chain alpha-keto acid dehydrogenase/2-oxoisovalerate dehydrogenase complex (BCADC). PDC catalyzes the irreversible oxidative decarboxylation of pyruvate to produce acetyl-CoA in the bridging step between glycolysis and the citric acid cycle. ADC participates in the breakdown of acetoin while BCADC participates in the breakdown of branched chain amino acids. BCADC catalyzes the oxidative decarboxylation of 4-methyl-2-oxopentanoate, 3-methyl-2-oxopentanoate and 3-methyl-2-oxobutanoate (branched chain 2-oxo acids derived from the transamination of leucine, valine and isoleucine).
Pssm-ID: 238958 [Multi-domain] Cd Length: 293 Bit Score: 45.95 E-value: 3.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 412 MPQAIGA----KATAPDRQVVAMCGDGGFSMlmGDF---LSLAQ-MKLPVKIVIFNNsvlgfvamemkagGY-----LTD 478
Cdd:cd02000 110 VPLAAGAalalKYRGEDRVAVCFFGDGATNE--GDFheaLNFAAlWKLPVIFVCENN-------------GYaistpTSR 174
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 640683833 479 GTelHATNFARIAEACGIKGIRV------ESASEVDEALQTAFATDGPVLVDVVV 527
Cdd:cd02000 175 QT--AGTSIADRAAAYGIPGIRVdgndvlAVYEAAKEAVERARAGGGPTLIEAVT 227
|
|
| TPP_IOR_alpha |
cd02008 |
Thiamine pyrophosphate (TPP) family, IOR-alpha subfamily, TPP-binding module; composed of ... |
407-523 |
4.08e-04 |
|
Thiamine pyrophosphate (TPP) family, IOR-alpha subfamily, TPP-binding module; composed of proteins similar to indolepyruvate ferredoxin oxidoreductase (IOR) alpha subunit. IOR catalyzes the oxidative decarboxylation of arylpyruvates, such as indolepyruvate or phenylpyruvate, which are generated by the transamination of aromatic amino acids, to the corresponding aryl acetyl-CoA.
Pssm-ID: 238966 [Multi-domain] Cd Length: 178 Bit Score: 41.49 E-value: 4.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 407 SMANAMPQAIGAKATAPDRQVVAMCGDGGFsMLMGdFLSLAQM---KLPVKIVIFNNSVlgfVAM----EMKAGGYLTDG 479
Cdd:cd02008 52 CMGASIGVAIGMAKASEDKKVVAVIGDSTF-FHSG-ILGLINAvynKANITVVILDNRT---TAMtggqPHPGTGKTLTE 126
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 640683833 480 TELHAtNFARIAEACGIKGIRV---ESASEVDEALQTAFATDGP-VLV 523
Cdd:cd02008 127 PTTVI-DIEALVRAIGVKRVVVvdpYDLKAIREELKEALAVPGVsVII 173
|
|
| PRK05778 |
PRK05778 |
2-oxoglutarate ferredoxin oxidoreductase subunit beta; Validated |
402-464 |
7.49e-04 |
|
2-oxoglutarate ferredoxin oxidoreductase subunit beta; Validated
Pssm-ID: 235604 [Multi-domain] Cd Length: 301 Bit Score: 41.79 E-value: 7.49e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 640683833 402 SFN--HGSManaMPQAIGAKATAPDRQVVAMCGDG-GFSMLMGDFLSLAQMKLPVKIVIFNNSVLG 464
Cdd:PRK05778 67 GLHtlHGRA---IAFATGAKLANPDLEVIVVGGDGdLASIGGGHFIHAGRRNIDITVIVENNGIYG 129
|
|
| TPP_OGFOR |
cd03375 |
Thiamine pyrophosphate (TPP family), 2-oxoglutarate ferredoxin oxidoreductase (OGFOR) ... |
405-526 |
1.39e-03 |
|
Thiamine pyrophosphate (TPP family), 2-oxoglutarate ferredoxin oxidoreductase (OGFOR) subfamily, TPP-binding module; OGFOR catalyzes the oxidative decarboxylation of 2-oxo-acids, with ferredoxin acting as an electron acceptor. In the TCA cycle, OGFOR catalyzes the oxidative decarboxylation of 2-oxoglutarate to succinyl-CoA. In the reductive tricarboxylic acid cycle found in the anaerobic autotroph Hydrogenobacter thermophilus, OGFOR catalyzes the reductive carboxylation of succinyl-CoA to produce 2-oxoglutarate. Thauera aromatica OGFOR has been shown to provide reduced ferredoxin to benzoyl-CoA reductase, a key enzyme in the anaerobic metabolism of aromatic compounds. OGFOR is dependent on TPP and a divalent metal cation for activity.
Pssm-ID: 239470 [Multi-domain] Cd Length: 193 Bit Score: 40.20 E-value: 1.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 405 HGsmaNAMPQAIGAKATAPDRQVVAMCGDG-GFSMLMGDFLSLAQMKLPVKIVIFNNSVLGfvameMKAG--------GY 475
Cdd:cd03375 53 HG---RALAVATGVKLANPDLTVIVVSGDGdLAAIGGNHFIHAARRNIDITVIVHNNQIYG-----LTKGqaspttpeGF 124
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 640683833 476 LT----DGTELHATNFARIAEACGikGIRVESASEVD-----EALQTAFATDGPVLVDVV 526
Cdd:cd03375 125 KTkttpYGNIEEPFNPLALALAAG--ATFVARGFSGDikqlkEIIKKAIQHKGFSFVEVL 182
|
|
| |
